His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis - Talwar - 2000 - European Journal of Biochemistry

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class="citation__page-range"> p. 1441-1446</span><a href="https://febs-onlinelibrary-wiley-com.translate.goog/journal/14321033?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" title="European Journal of Biochemistry homepage" class="citation--logo"><img id="journal-banner-image" test="test-value" alt="European Journal of Biochemistry" src="/pb-assets/journal-banners/14321033.jpg" class="journal-banner-image"></a> <script>var image = new Image(); image.onerror = function() { // if the image does not exist //document.getElementById("journal-banner-text").style.marginBottom = "15px"; document.getElementById("journal-banner-text").style.fontSize = "22px"; document.getElementById("journal-banner-image").style.display = "none"; } image.src = "/pb-assets/journal-banners/14321033.jpg";</script> </div> <div class="doi-access-container clearfix"> <span class="primary-heading"></span> <div class="doi-access-wrapper"> <div class="free-access access-type"> <i aria-hidden="true" class="icon-icon-lock_open"></i> <div class="doi-access"> Free Access </div> </div> </div> </div> <h1 class="citation__title">His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis</h1> <div class="pb-dropzone" data-pb-dropzone="publicaitonContent-versions">  </div> <div class="loa comma visible-xs mobile-authors loa-authors-trunc"> <div class="comma__list"> <span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Talwar/Rashmi?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="am1" data-db-target-for="am1" aria-controls="am1" aria-haspopup="true" id="am1_Ctrl" role="button"><span>Rashmi Talwar</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="am1" aria-labelledby="am1_Ctrl" role="region" id="am1"> <p class="author-name">Rashmi Talwar</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Talwar/Rashmi?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span><span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Jagath/Junutula+R.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="am2" data-db-target-for="am2" aria-controls="am2" aria-haspopup="true" id="am2_Ctrl" role="button"><span>Junutula R. Jagath</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="am2" aria-labelledby="am2_Ctrl" role="region" id="am2"> <p class="author-name">Junutula R. Jagath</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Jagath/Junutula+R.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span><span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Rao/N.+Appaji?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="am3" data-db-target-for="am3" aria-controls="am3" aria-haspopup="true" id="am3_Ctrl" role="button"><span>N. Appaji Rao</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="am3" aria-labelledby="am3_Ctrl" role="region" id="am3"> <p class="author-name">N. Appaji Rao</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Rao/N.+Appaji?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span><span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Savithri/H.+S.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="am4" data-db-target-for="am4" aria-controls="am4" aria-haspopup="true" id="am4_Ctrl" role="button"><span>H. S. Savithri</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="am4" aria-labelledby="am4_Ctrl" role="region" id="am4"> <p class="author-name">H. S. Savithri</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Savithri/H.+S.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span> </div> </div> <div class="loa-wrapper loa-authors hidden-xs desktop-authors"> <div id="sb-1" class="accordion"> <div class="comma__list"> <div class="accordion-tabbed"> <span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Talwar/Rashmi?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="a1" data-db-target-for="a1" aria-controls="a1" aria-haspopup="true" id="a1_Ctrl" role="button"><span>Rashmi Talwar</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="a1" aria-labelledby="a1_Ctrl" role="region" id="a1"> <p class="author-name">Rashmi Talwar</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Talwar/Rashmi?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span><span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Jagath/Junutula+R.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="a2" data-db-target-for="a2" aria-controls="a2" aria-haspopup="true" id="a2_Ctrl" role="button"><span>Junutula R. Jagath</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="a2" aria-labelledby="a2_Ctrl" role="region" id="a2"> <p class="author-name">Junutula R. Jagath</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Jagath/Junutula+R.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span><span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Rao/N.+Appaji?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="a3" data-db-target-for="a3" aria-controls="a3" aria-haspopup="true" id="a3_Ctrl" role="button"><span>N. Appaji Rao</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="a3" aria-labelledby="a3_Ctrl" role="region" id="a3"> <p class="author-name">N. Appaji Rao</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Rao/N.+Appaji?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span><span class="accordion-tabbed__tab-mobile accordion__closed"><a href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Savithri/H.+S.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="author-name accordion-tabbed__control" data-id="a4" data-db-target-for="a4" aria-controls="a4" aria-haspopup="true" id="a4_Ctrl" role="button"><span>H. S. Savithri</span><i aria-hidden="true" class="icon-section_arrow_d"></i></a><span class="comma-separator">, </span> <div class="author-info accordion-tabbed__content" data-db-target-of="a4" aria-labelledby="a4_Ctrl" role="region" id="a4"> <p class="author-name">H. S. Savithri</p> <p>Department of Biochemistry, Indian Institute of Science, Bangalore, India</p><a class="moreInfoLink" href="https://febs-onlinelibrary-wiley-com.translate.goog/authored-by/Savithri/H.+S.?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto">Search for more papers by this author</a> </div></span> </div> </div> </div> </div> <div class="epub-sections"> <div class="epub-section"> <span class="epub-state">First published: </span><span class="epub-date">25 December 2001</span> </div> <div class="epub-section"> <a class="epub-doi" aria-label="Digital Object Identifier for His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis link" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://doi.org/10.1046/j.1432-1327.2000.01142.x">https://doi.org/10.1046/j.1432-1327.2000.01142.x</a> </div> <div class="epub-section cited-by-count"> <span>Citations: <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#citedby-section">4</a></span> </div> </div> <div class="article-header__correspondence-to"> <i aria-hidden="true" class="at-icon-wrapper icon-mail_outline"></i> H. S. Savithri, Department of Biochemistry, Indian Institute of Science, Bangalore-560012, India. 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main abstractlang_en main">Abstract</h2> <div class="article-section__content en main"> <p>The three-dimensional structures of rabbit and human liver cytosolic serine hydroxymethyltransferase revealed that H231 interacts with the O3′ of pyridoxal-5′-phosphate and other residues at the active site such as S203, K257, H357 and R402 (numbering as per the human enzyme). This and the conserved nature of H231 in all serine hydroxymethyltransferases highlights its importance in catalysis and/or maintenance of oligomeric structure of the enzyme. In an attempt to decipher the role of H230 (H231 of the human enzyme) in the catalytic mechanism and/or maintenance of oligomeric structure of sheep liver serine hydroxymethyltransferase, the residue was mutated to arginine, phenylalanine, alanine, asparagine or tyrosine. Our results suggest that the nature of the amino acid substitution has a marked effect on the catalytic activity of the enzyme. H230R and H230F mutant proteins were completely inactive, dimeric and did not bind pyridoxal-5′-phosphate. On the other hand, mutation to alanine and asparagine retained the oligomeric structure and ability to bind pyridoxal-5′-phosphate. These mutants had only 2–3% catalytic activity. The side reactions like transamination and 5,6,7,8-tetrahydrofolate independent aldol cleavage were much more severely affected. They were able to form the external aldimine with glycine and serine but the quinonoid intermediate was not observed upon the addition of 5,6,7,8-tetrahydrofolate. Mutation to tyrosine did not affect the oligomeric structure and pyridoxal-5′-phosphate binding. The H230Y enzyme was 10% active and showed a correspondingly lower amount of quinonoid intermediate. The <i>k</i><sub>cat</sub> / <i>K</i><sub>m</sub> values for <span class="smallCaps">l</span>-serine and <span class="smallCaps">l</span><i>allo</i>threonine were 10-fold and 174-fold less for this mutant enzyme compared to the wild-type protein. These results suggest that H230 is involved in the step prior to the formation of the quinonoid intermediate, possibly in orienting the pyridine ring of the cofactor, in order to facilitate effective proton abstraction.</p> </div> </section> </div> <div class="pb-dropzone" data-pb-dropzone="below-abstract-group">  </div> <section class="article-section article-section__full"> <h3 class="list-paired__title">Abbreviations</h3> <div class="list-paired" id=""> <dl> <dt> <li>AATase</li> </dt> <dd> <li>asparatate aminotransferase</li> </dd> <dt> <li>hcSHMT</li> </dt> <dd> <li>human liver cytosolic SHMT</li> </dd> <dt> <li>H<sub>4</sub>-folate</li> </dt> <dd> <li>5,6,7,8-tetrahydrofolate</li> </dd> <dt> <li>MA</li> </dt> <dd> <li>methoxyamine</li> </dd> <dt> <li>PLP</li> </dt> <dd> <li>pyridoxal-5′-phosphate</li> </dd> <dt> <li>scSHMT</li> </dt> <dd> <li>sheep liver recombinant SHMT</li> </dd> <dt> <li>SHMT</li> </dt> <dd> <li>serine hydroxymethyltransferase</li> </dd> <dt> <li>TSC</li> </dt> <dd> <li>thiosemicarbazide</li> </dd> </dl> </div> <section class="article-section__content" id="s1-1-ps" lang="en"> <p>Serine hydroxymethyltransferase (SHMT, E.C.2.1.2.1), a pyridoxal-5′-phosphate dependent enzyme, catalyzes the conversion of serine and 5,6,7,8-tetrahydrofolate (H<sub>4</sub>-folate) to glycine and 5,10-methylene-H<sub>4</sub>-folate (5,10-CH<sub>2</sub>-H<sub>4</sub>-folate) [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b1" class="scrollableLink">1</a>]. Like other PLP-dependent enzymes, SHMT exhibits broad substrate and reaction specificity, as it also catalyzes H<sub>4</sub>-folate-independent aldolytic cleavage, decarboxylation, racemization and transamination reactions. The X-ray structure of the human liver cytosolic SHMT (hcSHMT) [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b2" class="scrollableLink">2</a>] revealed that the tetrameric protein was a ‘dimer of dimers’, stabilized by the N-terminal arm as suggested earlier by mutational studies on sheep liver cytosolic SHMT (scSHMT) [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b3" class="scrollableLink">3</a>]. PLP is bound to K257 as a Schiff's base linkage and is present at the interface of the tight dimers. The protonated N1 nitrogen of PLP is hydrogen bonded to D228, which, in turn, is bonded to H151. H231 is involved in hydrogen bonding interactions with the O3′ of PLP. In addition, it is within hydrogen-bonding distance of S203, K257, H357 and R402. The phosphate group of PLP is hydrogen bonded to various residues including Y73 and G303 from the neighboring subunit. More recently, Scarsdale <i>et al</i>. [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b4" class="scrollableLink">4</a>] reported the three-dimensional structure of rabbit liver cytosolic SHMT (rcSHMT), which confirms these features in the structure of SHMT. They have also examined in detail the implications of the structure to the catalytic mechanism of the reaction.</p> <p>Histidine, at position 230 of scSHMT (H231 of hcSHMT), is completely conserved in the primary structure of all SHMTs known so far [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b5" class="scrollableLink">5</a>]. The three-dimensional structure of aspartate aminotransferase (AATase) showed that a tyrosine was present at the equivalent position and was hydrogen bonded to the O3′ of PLP [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b6" class="scrollableLink">6</a>]. However, Y225 was conserved only in ≈ 70% of the AATase sequences known so far. H207 of 8-amino-7-oxononanoate synthase [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b7" class="scrollableLink">7</a>], A186 of serine-pyruvate aminotransferase, T319 of ornithine decarboxylase and Q246 of dialkylglycine decarboxylase [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b9" class="scrollableLink">9</a>] occupy positions equivalent to Y225 of AATase. The role of this residue in catalysis has not been examined in any of the above mentioned enzymes, except for AATase, in which a Y225R mutation led to a complete loss of transaminase activity [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b10" class="scrollableLink">10</a>]. It was therefore of interest to mutate H230 to arginine in analogy with the studies on AATase; to alanine, a conservative choice in mutational studies; to tyrosine, which mimics the situation in AATase; to phenylalanine, in order to decipher the role of the hydroxyl group; or to asparagine, which is a conservative mutation with steric effects similar to those of histidine but has a neutralized charge. The results obtained in this study clearly demonstrate that mutation of H230 leads to a dramatic reduction in the catalytic activity of SHMT and also changes in its oligomeric structure depending on the nature of the substitution.</p> </section> <section class="article-section__content" id="ss1" lang="en"> <h2 class="article-section__title section__title section1" id="ss1-title">Experimental procedures</h2> <p>Glycine, <span class="smallCaps">l</span>-serine, <span class="smallCaps">d</span>-alanine, NADH, β-phenylserine, 2-mercaptoethanol, folic acid, PLP, EDTA, aminooxyacetic acid, methoxyamine (MA), <span class="smallCaps">l</span>-aspartate, α-ketoglutarate and <span class="smallCaps">l</span><i>allo</i>threonine were obtained from Sigma Chemicals Co. St. Louis, MO, USA. [α-<sup>32</sup>P]dATP (3000 Ci·mmol<sup>−1</sup>) and <span class="smallCaps">l</span>-[3-<sup>14</sup>C]serine (55 mCi·mmol<sup>−1</sup>), restriction endonucleases (<i>Kpn</i>I, <i>Bam</i>HI and <i>Pml</i> I), Sequenase Version 2 DNA sequencing kit and DNA modifying enzymes (T<sub>4</sub> DNA ligase, Klenow fragment) were obtained from Amersham Pharmacia Biotech, Bucks, UK. [2-<sup>3</sup>H]Glycine (41.1 Ci·mmol<sup>−1</sup>) was purchased from NEN Life Science Products, Inc. Boston, MA, USA. <i>Pfu</i> polymerase was purchased from Stratagene and Deep Vent polymerase from New England Biolabs, Inc., Beverly, MA, USA. Sephacryl S-200, Superose 12 HR 10/30 were purchased from Pharmacia, Uppsala, Sweden. The oligonucleotide primers were custom synthesized by Bangalore Genei Pvt. Ltd, India. H<sub>4</sub>-Folate was prepared by the method of Hatefi <i>et al</i>. [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b11" class="scrollableLink">11</a>]. All other biochemicals used in this study were of the highest purity available.</p> <section class="article-section__sub-content" id="ss2" lang="en"> <h3 class="article-section__sub-title section2" id="ss2-title">Bacterial strains and growth conditions</h3> <p><i>Escherichia coli</i> DH5α was the recipient strain for the plasmids used in subcloning and sequencing. Strain BL21(DE3) pLysS [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b12" class="scrollableLink">12</a>] was used for bacterial expression of pET and pRSET constructs. CJ236 was the strain of choice for preparation of single strand DNA. Luria–Bertani medium or terrific broth with 50 µg·mL<sup>−1</sup> of ampicillin was used for growing <i>E. coli</i> cells.</p> </section> <section class="article-section__sub-content" id="ss3" lang="en"> <h3 class="article-section__sub-title section2" id="ss3-title">DNA manipulations</h3> <p>Plasmids were prepared by the alkaline lysis method as described by Sambrook <i>et al</i>. [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b13" class="scrollableLink">13</a>]. Restriction analysis and DNA ligations were carried out according to the manufacturer's instructions. Competent cells were prepared by the procedure of Alexander [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b14" class="scrollableLink">14</a>].</p> </section> <section class="article-section__sub-content" id="ss4" lang="en"> <h3 class="article-section__sub-title section2" id="ss4-title">Site-directed mutagenesis</h3> <p>All the H230 mutants except H230R were constructed by the PCR based megaprimer method [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b15" class="scrollableLink">15</a>,<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b16" class="scrollableLink">16</a>]. The oligonucleotides used for the generation of mutants are as follows: H230A, 5′-GAC ATG GCA GCG ATA TCC GGG CTG GTG GC-3′; H230F, 5′-C ATG GCA TTT ATC AGC GG-3′; H230N, 5′-AC ATG GCA AAT ATT AGC GGG CTG-3′; H230R, 5′-G GCT GAC ATG GCG CGC ATC AGC GGG C-3′; H230Y, 5′-AC ATG GCA TAT ATC AGC G-3′; M13 universal reverse primer (19-mer), 5′-GGA AAC AGC TAT GAC CAT G-3′; and SHP1 (19-mer), 5′-T ATG GCA GCT CCA GTC AAC-3′.</p> <p>The full length PCR product was subcloned into pUC19 at <i>Kpn</i>I and <i>Bam</i>HI sites. The clone was double digested with <i>Kpn</i>I and <i>Pml</i>I to obtain the 0.5 kb fragment that was swapped with the corresponding 0.5 kb fragment of the wild-type clone, i.e. pETSH (SHMT gene in pET 3c). The entire 0.5 kb region was sequenced using Sequenase Version 2 DNA sequencing kit to confirm the presence of the desired mutation and the absence of any nonspecific mutation(s). The H230R mutation was generated by the conventional Kunkel's method [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b17" class="scrollableLink">17</a>] using pGSH [SHMT gene subcloned in pGEM 3z f(–) vector] as a template. The product was similarly subcloned to obtain the mutant in the expression vector.</p> </section> <section class="article-section__sub-content" id="ss5" lang="en"> <h3 class="article-section__sub-title section2" id="ss5-title">Expression and purification of H230 mutant proteins</h3> <p>The scSHMT and the mutant enzymes were purified by the protocol described earlier [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b3" class="scrollableLink">3</a>]. Briefly, the BL21(DE3) pLysS extracts were subjected to ammonium sulphate fractionation, CM-Sephadex and Sephacryl S-200 column chromatography. The fractions were pooled and precipitated with 65% ammonium sulphate and the pellet was resuspended in Buffer A (50 m<span class="smallCaps">m</span> phosphate buffer, pH 7.4, 1 m<span class="smallCaps">m</span> EDTA and 1 m<span class="smallCaps">m</span> 2-mercaptoethanol). It was dialyzed against the same buffer with two changes and was used in all further studies. The amount of protein was estimated by the method of Lowry <i>et al</i>. [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b18" class="scrollableLink">18</a>].</p> </section> <section class="article-section__sub-content" id="ss6" lang="en"> <h3 class="article-section__sub-title section2" id="ss6-title">Enzyme assays</h3> <p>Aldol cleavage in the presence of H<sub>4</sub>-folate was monitored using <span class="smallCaps">l</span>-[3-<sup>14</sup>C]serine by the method of Manohar <i>et al</i>. [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b19" class="scrollableLink">19</a>]. Aldolytic cleavage of <span class="smallCaps">l</span><i>allo</i>threonine was monitored as described by Jagath <i>et al</i>. [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b20" class="scrollableLink">20</a>]. The rates of transamination of <span class="smallCaps">d</span>-alanine were determined as described earlier [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b21" class="scrollableLink">21</a>].</p> </section> <section class="article-section__sub-content" id="ss7" lang="en"> <h3 class="article-section__sub-title section2" id="ss7-title">Proton exchange studies</h3> <p>The proton exchange studies were carried out using tritiated glycine as described by Schirch and Jenkins [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b22" class="scrollableLink">22</a>].</p> </section> <section class="article-section__sub-content" id="ss8" lang="en"> <h3 class="article-section__sub-title section2" id="ss8-title">Spectral measurements</h3> <p>The absorbance spectra of the wild type and mutant enzymes (5 µ<span class="smallCaps">m</span>) were recorded in a Shimadzu UV 160 A spectrophotometer, both in the presence and absence of ligands and at different time intervals, when necessary. The oligomeric status of the proteins was determined using a calibrated Superose 12 HR 10/30 column attached to a Pharmacia FPLC system.</p> </section> <section class="article-section__sub-content" id="ss9" lang="en"> <h3 class="article-section__sub-title section2" id="ss9-title">Determination of association constants</h3> <p>The substrate induced quenching of fluorescence of enzyme bound PLP was monitored using a Jasco FP 777 spectrofluorimeter using a modified version of the protocol reported earlier [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b23" class="scrollableLink">23</a>].</p> </section> </section> <section class="article-section__content" id="ss10" lang="en"> <h2 class="article-section__title section__title section1" id="ss10-title">Results and discussion</h2> <p>Biochemical characterization of the H230 mutants of sheep liver SHMT showed that the nature of the substitution affects catalysis and oligomeric status to different extents. It is evident from <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#t1" class="scrollableLink">Table 1</a> that both H230A and H230N showed only 2–3% activity compared to scSHMT, and H230F and H230R exhibited a marked decrease (a thousand-fold) in activity. The H230Y mutant, however, showed ≈ 12% catalytic activity compared to scSHMT. Staining for activity upon native PAGE using β-phenylserine and 2,4-dinitrophenylhydrazine gave the characteristic yellow-orange band [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b24" class="scrollableLink">24</a>] only with scSHMT and not with the mutants (data not shown). Although the H230Y mutant exhibited ≈12% catalytic activity with serine as substrate, it did not give the yellow-orange band with β-phenylserine, probably because the method of activity staining is not sensitive enough to pick up small amounts of benzaldehyde formed.</p> <div class="article-table-content" id="t1"> <header class="article-table-caption"> <span class="table-caption__label">Table 1. </span><b>Catalytic efficiency and binding constants of the H230 mutants of scSHMT.</b> Specific activity is defined as the amount of HCHO (µmol) formed per min at 37 °C and pH 7.4. Binding constants of H230 mutants for <span class="smallCaps">l</span>-serine and glycine were determined by quenching of the fluorescence of the enzyme bound PLP </header> <div class="article-table-content-wrapper" tabindex="0"> <table class="table article-section__table"> <thead> <tr> <th class="bottom-bordered-cell left-aligned">Protein</th> <th class="bottom-bordered-cell left-aligned">Specific activity <br> (U·mg<sup>−1</sup>)</th> <th class="bottom-bordered-cell left-aligned">% Activity</th> <th class="bottom-bordered-cell left-aligned"><span class="smallCaps">l</span>-Serine <br> (m<span class="smallCaps">m</span>)</th> <th class="bottom-bordered-cell left-aligned">Glycine <br> (m<span class="smallCaps">m</span>)</th> </tr> </thead> <tbody> <tr> <td class="left-aligned">scSHMT</td> <td class="left-aligned">4.8</td> <td class="left-aligned">100</td> <td class="left-aligned">0.98</td> <td class="left-aligned">12.0</td> </tr> <tr> <td class="left-aligned">H230A</td> <td class="left-aligned">0.11</td> <td class="left-aligned">2</td> <td class="left-aligned">0.85</td> <td class="left-aligned">11.3</td> </tr> <tr> <td class="left-aligned">H230N</td> <td class="left-aligned">0.12</td> <td class="left-aligned">2</td> <td class="left-aligned">0.94</td> <td class="left-aligned">12.0</td> </tr> <tr> <td class="left-aligned">H230F</td> <td class="left-aligned">0.005</td> <td class="left-aligned">0.001</td> <td class="left-aligned">–</td> <td class="left-aligned">–</td> </tr> <tr> <td class="left-aligned">H230R</td> <td class="left-aligned">0.005</td> <td class="left-aligned">0.001</td> <td class="left-aligned">–</td> <td class="left-aligned">–</td> </tr> <tr> <td class="left-aligned">H230Y</td> <td class="left-aligned">0.52</td> <td class="left-aligned">11</td> <td class="left-aligned">0.86</td> <td class="left-aligned">12.2</td> </tr> </tbody> </table> </div> <div class="article-section__table-source"></div> </div> <section class="article-section__sub-content" id="ss11" lang="en"> <h3 class="article-section__sub-title section2" id="ss11-title">Spectral and catalytic properties of the H230 mutant enzymes</h3> <p>The far UV-CD spectra of all the mutant enzymes were essentially similar to scSHMT, indicating that the mutations may not have caused major alterations in the secondary structure (data not shown). The intrinsic tryptophan fluorescence emission spectra of all the H230 mutants, except H230Y, were similar to that of scSHMT (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f1">Fig. 1</a>, inset). The H230Y protein showed a red shift in the emission maximum compared to scSHMT, suggesting that a subtle change in the environment around the tryptophan residues may have occurred as a consequence of the mutation. The H230A, H230N and H230Y mutants exhibited characteristic absorbance at 425 nm (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f1">Fig. 1</a>, curve 1), whereas the H230R and H230F mutants showed very little absorbance at 425 nm when an equal amount of the protein (5 µ<span class="smallCaps">m</span>) was used to record the spectra (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f1">Fig. 1</a>, curve 2). Like scSHMT, the H230A, H230N and H230Y mutants contained one mol of PLP bound per subunit. The addition of glycine to scSHMT resulted in the formation of a geminal diamine (343 nm), external aldimine (425 nm) and a very small amount of the quinionoid intermediate (495 nm). The addition of glycine to H230Y also showed a small amount of geminal diamine (data not shown). The addition of H<sub>4</sub>-folate to a mixture of scSHMT and glycine (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f1">Fig. 1</a>, curve 5) and the H230Y mutant and glycine (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f1">Fig. 1</a>, curve 4) gave the characteristic quinonoid intermediate, but the amount of this with the H230Y mutant was less. However, unlike scSHMT, the H230A and H230N mutants did not exhibit the characteristic spectral intermediates upon the addition of glycine (100 m<span class="smallCaps">m</span>) followed by H<sub>4</sub>-folate (1.8 m<span class="smallCaps">m</span>). This observation suggests that a step prior to the formation of the quinonoid intermediate was probably affected in these two mutants. To identify this step, the catalytic mechanism was examined in detail. The formation of the external aldimine upon addition of the substrate serine/glycine is an early step in catalysis. The association constants for binding of serine and glycine to scSHMT and the H230A, H230N and H230Y mutant proteins were determined by measuring the substrate-induced fluorescence quenching of the enzyme-bound PLP (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#t1" class="scrollableLink">Table 1</a><b>)</b>. The <i>K</i><sub>A</sub> values for serine (≈1 m<span class="smallCaps">m</span>) and glycine (≈10 m<span class="smallCaps">m</span>) for all the mutants were similar to that for scSHMT and indicated that they were capable of binding the substrates. The <i>K</i><sub>A</sub> values for the H230R and H230F mutant proteins could not be determined as they did not contain PLP.</p> <section class="article-section__inline-figure"> <figure class="figure" id="f1"> <a target="_blank" href="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/2037b4aa-7489-4441-8458-574a05ecc521/ejb1142.f1.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto"> <picture> <source srcset="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/2037b4aa-7489-4441-8458-574a05ecc521/ejb1142.f1.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" media="(min-width: 1650px)"> <img class="figure__image" src="/cms/asset/2037b4aa-7489-4441-8458-574a05ecc521/ejb1142.f1.gif" data-lg-src="/cms/asset/2037b4aa-7489-4441-8458-574a05ecc521/ejb1142.f1.gif" alt="Details are in the caption following the image" title="Details are in the caption following the image" loading="lazy"> </picture></a> <figcaption class="figure__caption"> <div class="figure__caption__header"> <strong class="figure__title">Figure 1<span style="font-weight:normal"></span></strong> <div class="figure-extra"> <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#" class="open-figure-link">Open in figure viewer</a><a href="https://febs-onlinelibrary-wiley-com.translate.goog/action/downloadFigures?id=f1&partId&doi=10.1046/j.1432-1327.2000.01142.x&_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="ppt-figure-link"><i aria-hidden="true" class="icon-Icon_Download"></i><span>PowerPoint</span></a> </div> </div> <div class="figure__caption figure__caption-text"> <p><b>The visible absorption spectra of scSHMT and H230 mutants.</b> Visible absorption spectra of scSHMT and the H230A, H230N and H230Y mutants (line 1), and the H230F and H230R mutants (line 2) were recorded in a Shimadzu UV-160 A spectrophotometer using 5 µ<span class="smallCaps">m</span> protein in buffer A. The spectra were recorded upon addition of 100 m<span class="smallCaps">m</span> glycine (line 3) to scSHMT and the H230A, H230N and H230Y mutants followed by addition of 1.8 m<span class="smallCaps">m</span> H<sub>4</sub>-folate (line 3, H230A and H230N mutants; line 4, H230Y mutant; line 5, scSHMT). Inset, intrinsic tryptophan fluorescence of H230 mutants. Protein (0.5 µ<span class="smallCaps">m</span>) in buffer A was excited at 280 nm and the emission spectrum was recorded between 300 and 400 nm on a Jasco FP 777 spectrofluorimeter at 25 °C. scSHMT (––); H230A, H230F, H230N and H230R mutants (—); H230Y mutant (–·–).</p> </div> </figcaption> </figure> </section> <p>The abstraction of the proton from the external aldimine to generate the quinonoid intermediate is a stereospecific reaction and is enhanced by H<sub>4</sub>-folate [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b22" class="scrollableLink">22</a>]. Proton exchange studies carried out with tritiated glycine revealed that whereas the H230Y mutant showed 15% exchange compared to scSHMT, the H230A and H230N mutants showed only ≈ 2% exchange at 60 µ<span class="smallCaps">m</span> H<sub>4</sub>-folate (data not shown), which correlates well with their observed physiological activity. Due to limitations of the spectral absorbance measurements, the formation of a small amount of quinonoid intermediate with the H230A and H230N mutants, if any, cannot be ruled out. The R401A mutant enzyme, which does not catalyze proton exchange [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b25" class="scrollableLink">25</a>], was used as a negative control. The amount of proton exchange and the concentration of the quinonoid intermediate formed with the H230Y mutant (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f1">Fig. 1</a>) correlates well with the observed activity of the mutant, emphasizing that the affected step of catalysis, namely proton abstraction, is partially restored. These observations would suggest that the proton transfer step of catalysis is affected but not fully abolished as a consequence of the H230A, H230N or H230Y mutations.</p> <p>The effect of mutation on the alternative reactions such as H<sub>4</sub>-folate-independent aldolytic cleavage of <span class="smallCaps">l</span><i>allo</i>threonine is shown in <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#t2" class="scrollableLink">Table 2</a>. The <i>K</i><sub>m</sub> values for <span class="smallCaps">l</span>-a<i>llo</i>threonine remained unaltered but the <i>k</i><sub>cat</sub> values were reduced by two orders of magnitude. On the other hand, the rate of transamination of <span class="smallCaps">d</span>-alanine (200 m<span class="smallCaps">m</span>) was reduced by 50% for the H230Y mutant. The pseudo first-order rate constants for scSHMT and the H230Y mutant were 0.0028 s<sup>−1</sup> and 0.0012 s<sup>−1</sup>, respectively. The H230A and H230N proteins were unable to use <span class="smallCaps">d</span>-alanine or <span class="smallCaps">l</span><i>allo</i>threonine as substrates, implying a role for a well hydrogen-bonded H230 residue in the catalytic cycle of SHMT.</p> <div class="article-table-content" id="t2"> <header class="article-table-caption"> <span class="table-caption__label">Table 2. </span><b>Kinetic parameters for the H<sub>4</sub>-folate dependent and independent aldolytic cleavage catalyzed by H230Y SHMT.</b> The kinetic constants were evaluated by a double reciprocal plot of the rate of the reaction vs. varying substrate concentrations. </header> <div class="article-table-content-wrapper" tabindex="0"> <table class="table article-section__table"> <thead> <tr> <td class="left-aligned"></td> <th colspan="2" class="bottom-bordered-cell left-aligned"><i>K</i> <sub>m</sub> (m<span class="smallCaps">m</span>)</th> <th colspan="2" class="bottom-bordered-cell left-aligned"><i>k</i> <sub>cat</sub> (s<sup>−1</sup>)</th> <th colspan="2" class="bottom-bordered-cell left-aligned"><i>k</i> <sub>cat</sub>/<i>K</i><sub>m</sub> (m<span class="smallCaps">m</span><sup>−1</sup>·s<sup>−1</sup>)</th> </tr> <tr> <th class="bottom-bordered-cell left-aligned">Protein</th> <th class="bottom-bordered-cell left-aligned">scSHMT</th> <th class="bottom-bordered-cell left-aligned">H230Y</th> <th class="bottom-bordered-cell left-aligned">scSHMT</th> <th class="bottom-bordered-cell left-aligned">H230Y</th> <th class="bottom-bordered-cell left-aligned">scSHMT</th> <th class="bottom-bordered-cell left-aligned">H230Y</th> </tr> </thead> <tbody> <tr> <td class="left-aligned"><span class="smallCaps">l</span>-Serine</td> <td class="left-aligned">1.0</td> <td class="left-aligned">0.9</td> <td class="left-aligned">4.23</td> <td class="left-aligned">0.43</td> <td class="left-aligned">4.23</td> <td class="left-aligned">0.48</td> </tr> <tr> <td class="left-aligned"><span class="smallCaps">l</span> <i>Allo</i>threonine</td> <td class="left-aligned">1.25</td> <td class="left-aligned">3.0</td> <td class="left-aligned">4.15</td> <td class="left-aligned">0.058</td> <td class="left-aligned">3.32</td> <td class="left-aligned">0.019</td> </tr> </tbody> </table> </div> <div class="article-section__table-source"></div> </div> <p>The observation that the proton abstraction step of catalysis and the side reactions were significantly affected by the mutation of H230 prompted an examination of the reactivity of PLP at the active site using well characterized inhibitors of SHMT such as MA [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b26" class="scrollableLink">26</a>] and thiosemicarbazide (TSC) [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b27" class="scrollableLink">27</a>]. The interaction of MA with scSHMT and H230Y was monitored spectrally. The pseudo first-order rate constants for the reaction of MA (20 µ<span class="smallCaps">m</span>) with scSHMT and the H230Y mutant were 0.052 min<sup>−1</sup> and 0.026 min<sup>−1</sup>, respectively. Similar reduction in the rate of the reaction was observed with aminooxyacetic acid (data not shown) suggesting that there was an alteration in the reactivity of the PLP-Schiff's base in H230Y.</p> <p>These findings were further corroborated when the interaction of the proteins with TSC was examined. It was shown earlier that TSC is a slow but tight binding inhibitor of sheep liver SHMT [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b27" class="scrollableLink">27</a>]. An early intermediate generated upon the interaction of TSC with sheep liver SHMT had a spectral absorbance at 464 nm and 440 nm and the concentration of this intermediate reached a maximal value after ≈15 min of the reaction [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b27" class="scrollableLink">27</a>]. Thereafter, the intermediate decomposed slowly to yield the thiosemicarbazone. It was established that this intermediate was present at the active site and the proton abstraction at the C2 position was an important step in its formation [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b27" class="scrollableLink">27</a>]. Upon reaction with TSC, scSHMT showed a profile (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f2">Fig. 2B</a>) similar to that observed earlier for the native sheep liver SHMT [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b27" class="scrollableLink">27</a>]. Compared to scSHMT, the rates of formation of the TSC–quinonoid intermediate and its decomposition were rapid in the case of the H230Y mutant (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f2">Fig. 2A</a>). It was not possible to determine the rate constants for these reactions, with accuracy, using conventional spectroscopic methods. There was no change in the absorbance at 464 nm for scSHMT, upto 10 min of the reaction; however, after 5 min, the concentration of the intermediate had decreased substantially (80%) in case of the H230Y mutant. These observations led to the conclusion that there is probably a change in the orientation of the PLP ring upon mutation of H230 to tyrosine that leads to an alteration in the reaction of the enzyme with different ligands, analogous to the situation for AATase.</p> <section class="article-section__inline-figure"> <figure class="figure" id="f2"> <a target="_blank" href="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/55709164-16f7-479f-98a2-242732355dfc/ejb1142.f2.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto"> <picture> <source srcset="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/55709164-16f7-479f-98a2-242732355dfc/ejb1142.f2.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" media="(min-width: 1650px)"> <img class="figure__image" src="/cms/asset/55709164-16f7-479f-98a2-242732355dfc/ejb1142.f2.gif" data-lg-src="/cms/asset/55709164-16f7-479f-98a2-242732355dfc/ejb1142.f2.gif" alt="Details are in the caption following the image" title="Details are in the caption following the image" loading="lazy"> </picture></a> <figcaption class="figure__caption"> <div class="figure__caption__header"> <strong class="figure__title">Figure 2<span style="font-weight:normal"></span></strong> <div class="figure-extra"> <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#" class="open-figure-link">Open in figure viewer</a><a href="https://febs-onlinelibrary-wiley-com.translate.goog/action/downloadFigures?id=f2&partId&doi=10.1046/j.1432-1327.2000.01142.x&_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="ppt-figure-link"><i aria-hidden="true" class="icon-Icon_Download"></i><span>PowerPoint</span></a> </div> </div> <div class="figure__caption figure__caption-text"> <p><b>Interaction of scSHMT and the H230Y mutant with TSC.</b> Absorbance spectrum of the H230Y mutant (A) and scSHMT (B) (5 µ<span class="smallCaps">m</span>) upon addition of TSC (2 m<span class="smallCaps">m</span>) was recorded at 30 s intervals for 10 min at 37 °C. Representative spectra recorded at time intervals indicated are shown in the figure.</p> </div> </figcaption> </figure> </section> <p>An alteration in the T<sub>m</sub> values of the protein in the presence of serine has been correlated to the conversion of the enzyme from an ‘open’ to a ‘closed’ conformation [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b28" class="scrollableLink">28</a>]. There was no change in the T<sub>m</sub> values of the mutant enzymes upon addition of serine (54 ± 2 °C), unlike the wild-type enzyme, for which the addition of 100 m<span class="smallCaps">m l</span>-serine to the holoenzyme enhanced it's T<sub>m</sub> value from 54 °C to 63 °C. These results indicate that the mutant enzymes, although capable of binding the substrates (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#t1" class="scrollableLink">Table 1</a>), are unable to bring about the required conformational change, suggesting that they may be present in a partially closed conformation. The crystal structure of the Y225R mutant of AATase also showed the enzyme to be present in a partially closed conformation [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b10" class="scrollableLink">10</a>].</p> </section> <section class="article-section__sub-content" id="ss12" lang="en"> <h3 class="article-section__sub-title section2" id="ss12-title">Oligomeric status of the mutant proteins</h3> <p>It was shown earlier that mutation of residues involved in PLP interaction lead to the dissociation of the tetrameric structure of scSHMT[<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b29" class="scrollableLink">29</a>]. The observation that the H230F and H230R mutants did not have bound PLP whereas the H230A, H230N and H230Y mutants contained stoichiometric amounts of PLP (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f1">Fig. 1</a>) necessitated an examination of the oligomeric structure of the mutant proteins. The oligomeric status of the freshly purified mutant enzymes was determined on a calibrated Superose 12 HR 10/30 analytical gel filtration column. scSHMT and the H230A, H230N and H230Y mutants eluted as a single symmetrical peak corresponding to a <i>M</i><sub>r</sub> of ≈ 210 kDa, suggesting that these proteins were tetramers (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f3">Fig. 3</a>). This was confirmed by estimating the amount of PLP per subunit of the enzyme. The H230F and H230R mutant proteins, however, eluted as symmetrical peaks with a <i>M</i><sub>r</sub> corresponding to the dimeric form (≈ 110 kDa) of the enzyme. Removal of the bound cofactor from the H230A, H230N and H230Y mutant proteins by reaction with <span class="smallCaps">l</span>-cysteine gave the corresponding apoenzymes, which eluted as dimers, unlike the apoenzyme for scSHMT, which was predominantly a tetramer (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f3">Fig. 3</a>, inset, solid trace). The mutant apoenzymes could not be reconstituted to tetramers upon exogenous addition of PLP (50–500 µ<span class="smallCaps">m</span>) whereas apo scSHMT was converted to a tetramer that was fully active (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f3">Fig. 3</a>, inset, dashed trace).</p> <section class="article-section__inline-figure"> <figure class="figure" id="f3"> <a target="_blank" href="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/170f4cd9-a0df-4a3d-acd4-aa19060b8eb9/ejb1142.f3.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto"> <picture> <source srcset="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/170f4cd9-a0df-4a3d-acd4-aa19060b8eb9/ejb1142.f3.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" media="(min-width: 1650px)"> <img class="figure__image" src="/cms/asset/170f4cd9-a0df-4a3d-acd4-aa19060b8eb9/ejb1142.f3.gif" data-lg-src="/cms/asset/170f4cd9-a0df-4a3d-acd4-aa19060b8eb9/ejb1142.f3.gif" alt="Details are in the caption following the image" title="Details are in the caption following the image" loading="lazy"> </picture></a> <figcaption class="figure__caption"> <div class="figure__caption__header"> <strong class="figure__title">Figure 3<span style="font-weight:normal"></span></strong> <div class="figure-extra"> <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#" class="open-figure-link">Open in figure viewer</a><a href="https://febs-onlinelibrary-wiley-com.translate.goog/action/downloadFigures?id=f3&partId&doi=10.1046/j.1432-1327.2000.01142.x&_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="ppt-figure-link"><i aria-hidden="true" class="icon-Icon_Download"></i><span>PowerPoint</span></a> </div> </div> <div class="figure__caption figure__caption-text"> <p><b>Size-exclusion chromatography profiles of scSHMT and H230 mutants.</b> The proteins (0.125 mg·mL<sup>−1</sup>) were analyzed on a calibrated Superose 12 HR 10/30 column attached to a Pharmacia FPLC system. The inset shows the gel filtration profile of apo scSHMT (—) prepared by incubating the enzyme with 10 m<span class="smallCaps">m l</span>-cysteine followed by dialysis. The apoenzyme was reconstituted with 50 µ<span class="smallCaps">m</span> PLP at room temperature for 5 min (---). ‘T’ represents the tetrameric form of scSHMT and the H230A, H230N and H230Y mutants, and ‘D’ represents the dimeric form of the H230F and H230R mutant proteins. The standard molecular weight markers used for calibration were: apoferritin (440 000), β-amylase (200 000), yeast alcohol dehydrogenase (150 000), bovine serum albumin (66 000) and carbonic anhydrase (29 000). The column was equilibrated with buffer A containing 0.1 M KCl at a flow rate of 0.3 mL·min<sup>−1</sup>. The eluent was monitored at 280 nm.</p> </div> </figcaption> </figure> </section> <p>Enzymes are known to exert their functions not only through the chemical properties of the amino acid sidechains present at the active site but also through residues proximal to it. Charge distribution throughout the active site also facilitates catalysis by electrostatically guiding the substrate molecule into the active site. This theme has been observed recurrently not only in PLP-dependent enzymes [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b2" class="scrollableLink">2</a>,<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b7 #b8 #b9" class="scrollableLink">7–9</a>,<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b10" class="scrollableLink">10</a>] but also in other enzyme systems like pyruvate decarboxylase [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b30" class="scrollableLink">30</a>]. In the case of hcSHMT, it has been reported that H151 stabilizes, via hydrogen bonding, the negative charge on D228, which is crucial for determining the basicity of the N1 of PLP [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b2" class="scrollableLink">2</a>]. The interaction of PLP with the active site residues of scSHMT is depicted in <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f4">Fig. 4</a>, based on the available crystal structure coordinates (PDB accession number 1BJ4) of hcSHMT [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b2" class="scrollableLink">2</a>]. The X-ray structure of hcSHMT [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b2" class="scrollableLink">2</a>] revealed the presence of a large network of hydrogen bonding interactions at the active site (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#t3" class="scrollableLink">Table 3</a>). <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/H231" title="Link to external resource: H231">H231</a> (H230 in scSHMT) is within hydrogen bonding distance of four residues within the same subunit, namely, <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/O3" title="Link to external resource: O3">O3</a>′ of PLP (0.309 nm), the NH group of the internal aldimine of <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/K257" title="Link to external resource: K257">K257</a> (0.256 nm), <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/S203" title="Link to external resource: S203">S203</a> (0.344 nm) and <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/H357" title="Link to external resource: H357">H357</a> (0.363 nm). <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/R402" title="Link to external resource: R402">R402</a>, the residue binding the carboxyl group of serine, lies 0.32 nm away from <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/H231" title="Link to external resource: H231">H231</a>. The active site milieu is highly polar as it is surrounded by charged residues such as arginine, aspartic acid, histidine, etc. (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f4">Fig. 4</a>). It is obvious that <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/H230" title="Link to external resource: H230">H230</a> of scSHMT, which is equivalent to <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/H231" title="Link to external resource: H231">H231</a> of hcSHMT, along with the pyridine ring of PLP, <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/D227" title="Link to external resource: D227">D227</a> and <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/H150" title="Link to external resource: H150">H150</a>, forms a charge relay system for effective proton abstraction from the external aldimine. The mutation of <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/H230" title="Link to external resource: H230">H230</a> to alanine, phenylalanine, asparagine, arginine or tyrosine disturbs the charge relay by affecting the hydrogen-bond interaction with <a target="_blank" class="accessionId" href="https://translate.google.com/website?sl=auto&tl=en&hl=auto&u=https://www.ncbi.nlm.nih.gov/nuccore/O3" title="Link to external resource: O3">O3</a>′ of PLP and altering the orientation of the PLP ring, thus affecting catalysis to various extents.</p> <section class="article-section__inline-figure"> <figure class="figure" id="f4"> <a target="_blank" href="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/7e277b60-548e-4619-a337-caafcb8acfac/ejb1142.f4.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto"> <picture> <source srcset="https://febs-onlinelibrary-wiley-com.translate.goog/cms/asset/7e277b60-548e-4619-a337-caafcb8acfac/ejb1142.f4.gif?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" media="(min-width: 1650px)"> <img class="figure__image" src="/cms/asset/7e277b60-548e-4619-a337-caafcb8acfac/ejb1142.f4.gif" data-lg-src="/cms/asset/7e277b60-548e-4619-a337-caafcb8acfac/ejb1142.f4.gif" alt="Details are in the caption following the image" title="Details are in the caption following the image" loading="lazy"> </picture></a> <figcaption class="figure__caption"> <div class="figure__caption__header"> <strong class="figure__title">Figure 4<span style="font-weight:normal"></span></strong> <div class="figure-extra"> <a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#" class="open-figure-link">Open in figure viewer</a><a href="https://febs-onlinelibrary-wiley-com.translate.goog/action/downloadFigures?id=f4&partId&doi=10.1046/j.1432-1327.2000.01142.x&_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto" class="ppt-figure-link"><i aria-hidden="true" class="icon-Icon_Download"></i><span>PowerPoint</span></a> </div> </div> <div class="figure__caption figure__caption-text"> <p><b>Hypothetical charge relay system operating at the active site of scSHMT formulated on the basis of the X-ray structure of hcSHMT (PDB accession number 1BJ4).</b> H230 corresponds to H231 of hcSHMT. The graphics visualization program <span class="smallCaps">o</span> was used for measuring the distances [<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b31" class="scrollableLink">31</a>].</p> </div> </figcaption> </figure> </section> <div class="article-table-content" id="t3"> <header class="article-table-caption"> <span class="table-caption__label">Table 3. </span><b>Length of potential hydrogen bonds between cofactor and active site residues in hcSHMT (PDB accession number 1BJ4).</b> </header> <div class="article-table-content-wrapper" tabindex="0"> <table class="table article-section__table"> <thead> <tr> <th class="bottom-bordered-cell left-aligned">Protein group(s)</th> <th class="bottom-bordered-cell left-aligned">Hydrogen bond length (nm)</th> </tr> </thead> <tbody> <tr> <td class="left-aligned">PLP O3′–K257 NZ</td> <td class="left-aligned">0.256</td> </tr> <tr> <td class="left-aligned">PLP O3′–H231 Nδ1</td> <td class="left-aligned">0.309</td> </tr> <tr> <td class="left-aligned">PLP O3′–S203 Oγ</td> <td class="left-aligned">0.381</td> </tr> <tr> <td class="left-aligned">H231 Nε2–S203 O</td> <td class="left-aligned">0.344</td> </tr> <tr> <td class="left-aligned">H231 Nδ1–S203 O</td> <td class="left-aligned">0.344</td> </tr> <tr> <td class="left-aligned">H231 O–H357 Nε2</td> <td class="left-aligned">0.363</td> </tr> <tr> <td class="left-aligned">H231 Nε2–R402 NH1</td> <td class="left-aligned">0.327</td> </tr> <tr> <td class="left-aligned">D228 Oδ2–H151 Nε2</td> <td class="left-aligned">0.265</td> </tr> <tr> <td class="left-aligned">D228 Oδ2–PLP N1</td> <td class="left-aligned">0.276</td> </tr> </tbody> </table> </div> <div class="article-section__table-source"></div> </div> <p>An examination of the X-ray structure of hcSHMT revealed that mutation of H230 of scSHMT to arginine would lead to a strong repulsion between the newly introduced positive charge of arginine and the R402 present nearby at the active site. This would probably result in the disruption of the tetrameric structure. Biochemical studies reported in this paper are in conformity with this explanation (<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#f3">Fig. 3</a>).</p> <p>The introduction of a large hydrophobic residue like phenylalanine in the highly polar active site pocket would affect the overall environment leading to the dissociation of the tetramer, explaining the dimeric nature of the H230F mutant. In both these mutants, i.e. H230F and H230R, loss of tetrameric structure leads to loss of catalytic activity and PLP binding.</p> <p>Replacement of the H230 with asparagine, which is structurally similar to histidine, does not interfere with the active site interactions, although the hydrogen bond between O3′ of PLP and amide nitrogen of H230N is probably weakened. This, in turn, could seriously affect the electron withdrawing ability of the pyridinium nitrogen, thus leading to loss of catalytic activity. In the case of the H230A mutant, as alanine is a small residue it does not sterically interfere with the residues at the active site. Both H230A and H230N mutants retain the oligomeric structure; however, H230A would be unable to form a hydrogen bond with O3′ of PLP, thus affecting the charge relay system, leading to a drastic reduction in the catalytic efficiency.</p> <p>The H231 in hcSHMT (PDB code 1BJ4) was mutated to tyrosine using the program <span class="smallCaps">o</span>[<a href="https://febs-onlinelibrary-wiley-com.translate.goog/doi/10.1046/j.1432-1327.2000.01142.x?_x_tr_sl=auto&_x_tr_tl=en&_x_tr_hl=auto#b31" class="scrollableLink">31</a>] and the resulting contacts were measured. Replacement of H230 with tyrosine establishes a hydrogen-bonding interaction between the O3′ of PLP and the OH group of tyrosine. This hydrogen bond is stronger than that with H230 as the distance between the two atoms decreases to 0.246 nm compared to 0.309 nm in the wild-type protein. However, this interaction decreases the bond distance between O3′ of PLP and the OH group of S203 (0.137 nm compared to 0.381 nm in wild-type protein). In order to accommodate a tyrosine residue more effectively in the active site, S203 had to be rotated away from the O3′ of PLP, disrupting the hydrogen bonding originally present in the wild-type enzyme. An important consequence of such a change could be that the basicity of N1 of PLP would be altered, thereby partially disrupting the charge relay system and affecting catalysis. Confirmation of these explanations, however, has to await the elucidation of the three-dimensional structure of the H230 mutants of SHMT.</p> <p>The results presented above demonstrate that H230, which is hydrogen bonded to O3′ of PLP and is part of a charge relay system, facilitates effective proton abstraction, an important event in the catalytic cycle of SHMT.</p> </section> </section> <section class="article-section__content" id="ss13" lang="en"> <h2 class="article-section__title section__title section1" id="ss13-title">Acknowledgements</h2> <p>This work was funded by the Department of Biotechnology, New Delhi, India and the CSIR Emeritus Scientist grant awarded to N.A.R. We thank Prof. M. R. N. Murthy and Mr S. Parthasarathy of MBU, IISc. for help with the modeling studies. The DBT protein and peptide sequencing facility is gratefully acknowledged for the N-terminal sequence analysis. Thanks are also due to Mr Jomon Joseph, Mr J. V. 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His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis - Talwar - 2000 - European Journal of Biochemistry - Wiley Online Library