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mw-first-heading"><small>DD</small>-Transpeptidase</h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 11 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-11" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">11 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Transpeptidasa" title="Transpeptidasa – Catalan" lang="ca" hreflang="ca" data-title="Transpeptidasa" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/Transpeptid%C3%A1za" title="Transpeptidáza – Czech" lang="cs" hreflang="cs" data-title="Transpeptidáza" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target"><span>Čeština</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/D-Alanin-Transpeptidase" title="D-Alanin-Transpeptidase – German" lang="de" hreflang="de" data-title="D-Alanin-Transpeptidase" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target"><span>Deutsch</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Transpeptidasa" title="Transpeptidasa – Spanish" lang="es" hreflang="es" data-title="Transpeptidasa" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Transpeptidase" title="Transpeptidase – French" lang="fr" hreflang="fr" data-title="Transpeptidase" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/DD-transpeptidase" title="DD-transpeptidase – Galician" lang="gl" hreflang="gl" data-title="DD-transpeptidase" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Transpeptidasi" title="Transpeptidasi – Italian" lang="it" hreflang="it" data-title="Transpeptidasi" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-he mw-list-item"><a href="https://he.wikipedia.org/wiki/%D7%98%D7%A8%D7%A0%D7%A1%D7%A4%D7%A4%D7%98%D7%99%D7%93%D7%90%D7%96" title="טרנספפטידאז – Hebrew" lang="he" hreflang="he" data-title="טרנספפטידאז" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target"><span>עברית</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/DD-transpeptidase" title="DD-transpeptidase – Dutch" lang="nl" hreflang="nl" data-title="DD-transpeptidase" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Serin-tip_D-Ala-D-Ala_karboksipeptidaza" title="Serin-tip D-Ala-D-Ala karboksipeptidaza – Serbian" lang="sr" hreflang="sr" data-title="Serin-tip D-Ala-D-Ala karboksipeptidaza" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Serin-tip_D-Ala-D-Ala_karboksipeptidaza" title="Serin-tip D-Ala-D-Ala karboksipeptidaza – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Serin-tip D-Ala-D-Ala karboksipeptidaza" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li> </ul> <div class="after-portlet after-portlet-lang"><span class="wb-langlinks-edit wb-langlinks-link"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q420272#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></span></div> </div> </div> </div> </header> <div class="vector-page-toolbar"> <div class="vector-page-toolbar-container"> <div id="left-navigation"> <nav 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screen{html.skin-theme-clientpref-night .mw-parser-output .infobox-full-data:not(.notheme)>div:not(.notheme)[style]{background:#1f1f23!important;color:#f8f9fa}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .infobox-full-data:not(.notheme) div:not(.notheme){background:#1f1f23!important;color:#f8f9fa}}@media(min-width:640px){body.skin--responsive .mw-parser-output .infobox-table{display:table!important}body.skin--responsive .mw-parser-output .infobox-table>caption{display:table-caption!important}body.skin--responsive .mw-parser-output .infobox-table>tbody{display:table-row-group}body.skin--responsive .mw-parser-output .infobox-table tr{display:table-row!important}body.skin--responsive .mw-parser-output .infobox-table th,body.skin--responsive .mw-parser-output .infobox-table td{padding-left:inherit;padding-right:inherit}}</style><table class="infobox"><tbody><tr><th colspan="2" class="infobox-above">Serine-type <small>D</small>-Ala-<small>D</small>-Ala carboxypeptidase</th></tr><tr><td colspan="2" class="infobox-image"><span class="mw-default-size" typeof="mw:File/Frameless"><a href="/wiki/File:DD-Transpeptidase.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a8/DD-Transpeptidase.png/220px-DD-Transpeptidase.png" decoding="async" width="220" height="165" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/a8/DD-Transpeptidase.png/330px-DD-Transpeptidase.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/a8/DD-Transpeptidase.png/440px-DD-Transpeptidase.png 2x" data-file-width="640" data-file-height="480" /></a></span><div class="infobox-caption">Structure of the streptomyces K15 <small>DD</small>-transpeptidase</div></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Identifiers</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC no.</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.enzyme-database.org/query.php?ec=3.4.16.4">3.4.16.4</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/CAS_registry_number" class="mw-redirect" title="CAS registry number">CAS no.</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://commonchemistry.cas.org/detail?cas_rn=9077-67-2&title=">9077-67-2 </a></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Databases</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/IntEnz" title="IntEnz">IntEnz</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=3.4.16.4">IntEnz view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/BRENDA" title="BRENDA">BRENDA</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://www.brenda-enzymes.org/enzyme.php?ecno=3.4.16.4">BRENDA entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/ExPASy" class="mw-redirect" title="ExPASy">ExPASy</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://enzyme.expasy.org/EC/3.4.16.4">NiceZyme view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/KEGG" title="KEGG">KEGG</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.genome.jp/dbget-bin/www_bget?enzyme+3.4.16.4">KEGG entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/MetaCyc" title="MetaCyc">MetaCyc</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://biocyc.org/META/substring-search?type=NIL&object=3.4.16.4">metabolic pathway</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/PRIAM_enzyme-specific_profiles" title="PRIAM enzyme-specific profiles">PRIAM</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://priam.prabi.fr/cgi-bin/PRIAM_profiles_CurrentRelease.pl?EC=3.4.16.4">profile</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a> structures</th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.rcsb.org/search?q=rcsb_polymer_entity.rcsb_ec_lineage.id:3.4.16.4">RCSB PDB</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/entry/search/index?ec_number:3.4.16.4">PDBe</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=3.4.16.4">PDBsum</a></td></tr><tr><td colspan="2" class="infobox-full-data" style="background-color: #eee"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1257001546"><table class="infobox mw-collapsible mw-collapsed" style="float:none; clear:none; margin:0; border-width:0; border-collapse:collapse; text-align:left; width:100%"><tbody><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Search</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/PubMed_Central" title="PubMed Central">PMC</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=3.4.16.4%5BEC/RN%20Number%5D%20AND%20pubmed%20pmc%20local%5Bsb%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/PubMed" title="PubMed">PubMed</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=3.4.16.4%5BEC/RN%20Number%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/National_Center_for_Biotechnology_Information" title="National Center for Biotechnology Information">NCBI</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/protein?term=3.4.16.4%5BEC/RN%20Number%5D">proteins</a></td></tr></tbody></table></td></tr></tbody></table> <p><b><small>DD</small>-Transpeptidase</b> (<a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> <a rel="nofollow" class="external text" href="https://enzyme.expasy.org/EC/3.4.16.4">3.4.16.4</a>, <i><small>DD</small>-peptidase</i>, <i><small>DD</small>-transpeptidase</i>, <i><small>DD</small>-carboxypeptidase</i>, <i><small>D</small>-alanyl-<small>D</small>-alanine <a href="/wiki/Carboxypeptidase" title="Carboxypeptidase">carboxypeptidase</a></i>, <i><small>D</small>-alanyl-<small>D</small>-alanine-cleaving-peptidase</i>, <i><small>D</small>-alanine carboxypeptidase</i>, <i><small>D</small>-alanyl carboxypeptidase</i>, and <i>serine-type <small>D</small>-Ala-<small>D</small>-Ala carboxypeptidase</i>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>) is a bacterial enzyme that catalyzes the transfer of the R-<small>L</small>-αα-<small>D</small>-alanyl <a href="/wiki/Moiety_(chemistry)" title="Moiety (chemistry)">moiety</a> of R-<small>L</small>-αα-<small>D</small>-alanyl-<small>D</small>-alanine carbonyl donors to the γ-OH of their active-site serine and from this to a final acceptor.<sup id="cite_ref-PMID7733866_2-0" class="reference"><a href="#cite_note-PMID7733866-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> </p><p>The <a href="/wiki/Antibiotic" title="Antibiotic">antibiotic</a> <a href="/wiki/Penicillin" title="Penicillin">penicillin</a> irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl-enzyme intermediate.<sup id="cite_ref-Gordon_2000_4-0" class="reference"><a href="#cite_note-Gordon_2000-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Because of the interaction between penicillin and transpeptidase, this enzyme is also known as <a href="/wiki/Penicillin-binding_protein" class="mw-redirect" title="Penicillin-binding protein">penicillin-binding protein</a> (PBP). </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Mechanism">Mechanism</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=DD-Transpeptidase&action=edit&section=1" title="Edit section: Mechanism"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><small>DD</small>-Transpeptidase is mechanistically similar to the proteolytic reactions of the trypsin protein family.<sup id="cite_ref-pmid12456788_5-0" class="reference"><a href="#cite_note-pmid12456788-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> </p> <figure class="mw-halign-center" typeof="mw:File/Thumb"><a href="/wiki/File:DD-Transpeptidase_mechanism_fixed.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/0/09/DD-Transpeptidase_mechanism_fixed.png/501px-DD-Transpeptidase_mechanism_fixed.png" decoding="async" width="501" height="411" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/0/09/DD-Transpeptidase_mechanism_fixed.png/752px-DD-Transpeptidase_mechanism_fixed.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/0/09/DD-Transpeptidase_mechanism_fixed.png/1002px-DD-Transpeptidase_mechanism_fixed.png 2x" data-file-width="2151" data-file-height="1766" /></a><figcaption>DD-transpeptidase catalytic mechanism</figcaption></figure> <p>Crosslinking of peptidyl <a href="/wiki/Moiety_(chemistry)" title="Moiety (chemistry)">moieties</a> of adjacent <a href="/wiki/Glycan" title="Glycan">glycan</a> strands is a two-step reaction. The first step involves the cleavage of the <small>D</small>-alanyl-<small>D</small>-alanine bond of a peptide unit precursor acting as carbonyl donor, the release of the carboxyl-terminal <small>D</small>-alanine, and the formation of the acyl-enzyme. The second step involves the breakdown of the acyl-enzyme intermediate and the formation of a new peptide bond between the carbonyl of the <small>D</small>-alanyl moiety and the amino group of another peptide unit.<sup id="cite_ref-Fonzé_1999_6-0" class="reference"><a href="#cite_note-Fonzé_1999-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p><p>Most discussion of <small>DD</small>-peptidase mechanisms revolves around the catalysts of proton transfer. During formation of the acyl-enzyme intermediate, a proton must be removed from the active site serine hydroxyl group and one must be added to the amine leaving group. A similar proton movement must be facilitated in deacylation. The identity of the general acid and base catalysts involved in these proton transfers has not yet been elucidated.<sup id="cite_ref-Pratt_2008_7-0" class="reference"><a href="#cite_note-Pratt_2008-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> However, the catalytic triad tyrosine, lysine, and serine, as well as serine, lysine, serine have been proposed.<sup id="cite_ref-Pratt_2008_7-1" class="reference"><a href="#cite_note-Pratt_2008-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Structure">Structure</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=DD-Transpeptidase&action=edit&section=2" title="Edit section: Structure"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Transpeptidases are members of the penicilloyl-serine transferase <a href="/wiki/Protein_superfamily" title="Protein superfamily">superfamily</a>, which has a signature SxxK conserved <a href="/wiki/Sequence_motif" title="Sequence motif">motif</a>.<sup id="cite_ref-Walsh_2016_8-0" class="reference"><a href="#cite_note-Walsh_2016-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> With "x" denoting a variable <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> residue, the transpeptidases of this superfamily show a trend in the form of three motifs: SxxK, SxN (or analogue), and KTG (or analogue). These motifs occur at equivalent places, and are roughly equally spaced, along the polypeptide chain. The folded protein brings these motifs close to each other at the catalytic center between an <a href="/wiki/Protein_fold_class" title="Protein fold class">all-α domain</a> and an <a href="/wiki/Protein_fold_class" title="Protein fold class">α/β domain</a>.<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> </p><p>The structure of the <a href="/wiki/Streptomyces" title="Streptomyces">streptomyces</a> K15 <small>DD</small>-transpeptidase has been studied, and consists of a single polypeptide chain organized into two domains. One domain contains mainly α-helices, and the second one is of α/β-type.<sup id="cite_ref-Fonzé_1999_6-1" class="reference"><a href="#cite_note-Fonzé_1999-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> The center of the catalytic cleft is occupied by the Ser35-Thr36-Thr37-Lys38 tetrad, which includes the nucleophilic Ser35 residue at the amino-terminal end of helix α2. One side of the cavity is defined by the Ser96-Gly97-Cys98 loop connecting helices α4 and α5. The Lys213-Thr214-Gly215 triad lies on strand β3 on the opposite side of the cavity. The backbone NH group of the essential Ser35 residue and that of Ser216 downstream from the motif Lys213-Thr214-Gly215 occupy positions that are compatible with the <a href="/wiki/Oxyanion_hole" title="Oxyanion hole">oxyanion hole</a> function required for catalysis.<sup id="cite_ref-Fonzé_1999_6-2" class="reference"><a href="#cite_note-Fonzé_1999-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p><p>The enzyme is classified as a <small>DD</small>-transpeptidase because the susceptible peptide bond of the carbonyl donor extends between two carbon atoms with the <small>D</small>-configuration.<sup id="cite_ref-Fonzé_1999_6-3" class="reference"><a href="#cite_note-Fonzé_1999-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Biological_Function">Biological Function</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=DD-Transpeptidase&action=edit&section=3" title="Edit section: Biological Function"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>All bacteria possess at least one, most often several, monofunctional serine <small>DD</small>-peptidases.<sup id="cite_ref-PMID7733866_2-1" class="reference"><a href="#cite_note-PMID7733866-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Disease_Relevance">Disease Relevance</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=DD-Transpeptidase&action=edit&section=4" title="Edit section: Disease Relevance"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Penicillin_vs_PG_terminus_structure.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/ce/Penicillin_vs_PG_terminus_structure.png/374px-Penicillin_vs_PG_terminus_structure.png" decoding="async" width="374" height="187" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/ce/Penicillin_vs_PG_terminus_structure.png/561px-Penicillin_vs_PG_terminus_structure.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/ce/Penicillin_vs_PG_terminus_structure.png/748px-Penicillin_vs_PG_terminus_structure.png 2x" data-file-width="1676" data-file-height="837" /></a><figcaption>The structural similarity between (A) <small>D</small>-Ala-<small>D</small>-Ala terminus of peptidoglycan terminus and (B) penicillins. Transpeptidases misrecognize penicillins for the TPase catalytic reaction.</figcaption></figure> <p>This enzyme is an excellent drug target because it is essential, is accessible from the <a href="/wiki/Periplasm" title="Periplasm">periplasm</a>, and has no equivalent in mammalian cells. <small>DD</small>-Transpeptidase is the target protein of <a href="/wiki/%CE%92-lactam_antibiotic" class="mw-redirect" title="Β-lactam antibiotic">β-lactam antibiotics</a> (e.g. <a href="/wiki/Penicillin" title="Penicillin">penicillin</a>). This is because the structure of the β-lactam closely resembles the <small>D</small>-ala-<small>D</small>-ala residue. </p><p>β-Lactams exert their effect by competitively inactivating the serine <small>DD</small>-transpeptidase catalytic site. Penicillin is a cyclic analogue of the <small>D</small>-Ala-<small>D</small>-Ala terminated carbonyl donors, therefore in the presence of this antibiotic, the reaction stops at the level of the serine ester-linked penicilloyl enzyme.<sup id="cite_ref-pmid7181854_11-0" class="reference"><a href="#cite_note-pmid7181854-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Thus β-lactam antibiotics force these enzymes to behave like <a href="/wiki/Penicillin_binding_proteins" class="mw-redirect" title="Penicillin binding proteins">penicillin binding proteins</a>.<sup id="cite_ref-Ghuysen_1984_12-0" class="reference"><a href="#cite_note-Ghuysen_1984-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p><p>Kinetically, the interaction between the <small>DD</small>-peptidase and β-lactams is a three-step reaction: </p><p><span class="mwe-math-element"><span class="mwe-math-mathml-inline mwe-math-mathml-a11y" style="display: none;"><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle E+I\rightleftharpoons E\cdot I\rightarrow E-I*\rightarrow E+P}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mi>E</mi> <mo>+</mo> <mi>I</mi> <mo class="MJX-variant" stretchy="false">⇌</mo> <mi>E</mi> <mo>⋅</mo> <mi>I</mi> <mo stretchy="false">→</mo> <mi>E</mi> <mo>−</mo> <mi>I</mi> <mo>∗</mo> <mo stretchy="false">→</mo> <mi>E</mi> <mo>+</mo> <mi>P</mi> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle E+I\rightleftharpoons E\cdot I\rightarrow E-I*\rightarrow E+P}</annotation> </semantics> </math></span><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/c43eaa8f374ced93175365e294d55b50e0438417" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.505ex; width:34.568ex; height:2.343ex;" alt="{\displaystyle E+I\rightleftharpoons E\cdot I\rightarrow E-I*\rightarrow E+P}"></span><sup id="cite_ref-Ghuysen_1984_12-1" class="reference"><a href="#cite_note-Ghuysen_1984-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p><p>β-Lactams may form an adduct E-I* of high stability with <span class="nowrap"><small>DD</small>-transpeptidase</span>. The half life of this adduct is around hours, whereas the half-life of the normal reaction is in the order of milliseconds.<sup id="cite_ref-Walsh_2016_8-1" class="reference"><a href="#cite_note-Walsh_2016-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p><p>The interference with the enzyme processes responsible for cell wall formation results in cellular lysis and death due to the triggering of the autolytic system in the bacteria.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=DD-Transpeptidase&action=edit&section=5" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Vancomycin" title="Vancomycin">Vancomycin</a>, an antibiotic that binds the <small>D</small>-ala-<small>D</small>-ala residues, inhibiting elongation via <a href="/wiki/Glycosyltransferase" title="Glycosyltransferase">glycosyltransferase</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=DD-Transpeptidase&action=edit&section=6" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist reflist-columns references-column-width" style="column-width: 32em;"> <ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite class="citation web cs1"><a rel="nofollow" class="external text" href="https://web.archive.org/web/20060517131821/http://www.biochem.ucl.ac.uk/bsm/enzymes/ec3/ec04/ec16/ec0004/index.html">"E.C.3.4.16.4 Serine-type D-Ala-D-Ala carboxypeptidase"</a>. <i>Enzyme Structures Database</i>. Archived from <a rel="nofollow" class="external text" href="http://www.biochem.ucl.ac.uk/bsm/enzymes/ec3/ec04/ec16/ec0004/index.html">the original</a> on May 17, 2006<span class="reference-accessdate">. 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class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7181854">7181854</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Biochemical+Journal&rft.atitle=Isolation+of+the+membrane-bound+26+000-Mr+penicillin-binding+protein+of+Streptomyces+strain+K15+in+the+form+of+a+penicillin-sensitive+D-alanyl-D-alanine-cleaving+transpeptidase&rft.volume=207&rft.issue=1&rft.pages=109-15&rft.date=1982-10&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1153830%23id-name%3DPMC&rft_id=info%3Apmid%2F7181854&rft_id=info%3Adoi%2F10.1042%2Fbj2070109&rft.aulast=Nguyen-Dist%C3%A8che&rft.aufirst=M&rft.au=Leyh-Bouille%2C+M&rft.au=Ghuysen%2C+JM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1153830&rfr_id=info%3Asid%2Fen.wikipedia.org%3ADD-Transpeptidase" class="Z3988"></span></span> </li> <li id="cite_note-Ghuysen_1984-12"><span class="mw-cite-backlink">^ <a href="#cite_ref-Ghuysen_1984_12-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Ghuysen_1984_12-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFGhuysenFrèreLeyh-BouilleNguyen-Distèche1984" class="citation journal cs1">Ghuysen JM, Frère JM, Leyh-Bouille M, Nguyen-Distèche M, Coyette J, Dusart J, Joris B, Duez C, Dideberg O, Charlier P (1984). "Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics". <i>Scandinavian Journal of Infectious Diseases. Supplementum</i>. <b>42</b>: 17–37. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/6597561">6597561</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Scandinavian+Journal+of+Infectious+Diseases.+Supplementum&rft.atitle=Bacterial+wall+peptidoglycan%2C+DD-peptidases+and+beta-lactam+antibiotics&rft.volume=42&rft.pages=17-37&rft.date=1984&rft_id=info%3Apmid%2F6597561&rft.aulast=Ghuysen&rft.aufirst=JM&rft.au=Fr%C3%A8re%2C+JM&rft.au=Leyh-Bouille%2C+M&rft.au=Nguyen-Dist%C3%A8che%2C+M&rft.au=Coyette%2C+J&rft.au=Dusart%2C+J&rft.au=Joris%2C+B&rft.au=Duez%2C+C&rft.au=Dideberg%2C+O&rft.au=Charlier%2C+P&rfr_id=info%3Asid%2Fen.wikipedia.org%3ADD-Transpeptidase" class="Z3988"></span></span> </li> <li id="cite_note-13"><span class="mw-cite-backlink"><b><a href="#cite_ref-13">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFSpratt1983" class="citation journal cs1">Spratt BG (May 1983). <a rel="nofollow" class="external text" href="https://doi.org/10.1099%2F00221287-129-5-1247">"Penicillin-binding proteins and the future of beta-lactam antibiotics. The Seventh Fleming Lecture"</a>. <i>Journal of General Microbiology</i>. <b>129</b> (5): 1247–60. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1099%2F00221287-129-5-1247">10.1099/00221287-129-5-1247</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/6352855">6352855</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+General+Microbiology&rft.atitle=Penicillin-binding+proteins+and+the+future+of+beta-lactam+antibiotics.+The+Seventh+Fleming+Lecture&rft.volume=129&rft.issue=5&rft.pages=1247-60&rft.date=1983-05&rft_id=info%3Adoi%2F10.1099%2F00221287-129-5-1247&rft_id=info%3Apmid%2F6352855&rft.aulast=Spratt&rft.aufirst=BG&rft_id=https%3A%2F%2Fdoi.org%2F10.1099%252F00221287-129-5-1247&rfr_id=info%3Asid%2Fen.wikipedia.org%3ADD-Transpeptidase" class="Z3988"></span></span> </li> </ol></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=DD-Transpeptidase&action=edit&section=7" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li>The <a href="/wiki/MEROPS" title="MEROPS">MEROPS</a> online database for peptidases and their inhibitors: <a rel="nofollow" class="external text" href="http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=S11.001">S11.001</a></li> <li><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> <a rel="nofollow" class="external text" href="https://enzyme.expasy.org/EC/3.4.16.4">3.4.16.4</a></li> <li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Serine-Type+D-Ala-D-Ala+Carboxypeptidase">Serine-Type+D-Ala-D-Ala+Carboxypeptidase</a> at the U.S. National Library of Medicine <a href="/wiki/Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist 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td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Hydrolase:_proteases_(EC_3.4)" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><style data-mw-deduplicate="TemplateStyles:r1239400231">.mw-parser-output .navbar{display:inline;font-size:88%;font-weight:normal}.mw-parser-output .navbar-collapse{float:left;text-align:left}.mw-parser-output .navbar-boxtext{word-spacing:0}.mw-parser-output .navbar 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href="/wiki/Template:Proteases" title="Template:Proteases"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Proteases" title="Template talk:Proteases"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Proteases" title="Special:EditPage/Template:Proteases"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Hydrolase:_proteases_(EC_3.4)" style="font-size:114%;margin:0 4em"><a href="/wiki/Hydrolase" title="Hydrolase">Hydrolase</a>: <a href="/wiki/Protease" title="Protease">proteases</a> (<a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> 3.4)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.11_Aminopeptidases" title="List of EC numbers (EC 3)">3.4.11</a>-19: <a href="/wiki/Exopeptidase" title="Exopeptidase">Exopeptidase</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.11_Aminopeptidases" title="List of EC numbers (EC 3)">3.4.11</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Aminopeptidase" title="Aminopeptidase">Aminopeptidase</a> <ul><li><a href="/wiki/Alanine_aminopeptidase" title="Alanine aminopeptidase">Alanine</a></li> <li><a href="/wiki/RNPEP" title="RNPEP">Arginyl</a></li> <li><a href="/wiki/DNPEP" title="DNPEP">Aspartyl</a></li> <li><a href="/wiki/Cystinyl_aminopeptidase" class="mw-redirect" title="Cystinyl aminopeptidase">Cystinyl</a></li> <li><a href="/wiki/Leucyl_aminopeptidase" title="Leucyl aminopeptidase">Leucyl</a></li> <li><a href="/wiki/Glutamyl_aminopeptidase" title="Glutamyl aminopeptidase">Glutamyl</a></li> <li><i>Methionyl</i> <ul><li><a href="/wiki/METAP1" title="METAP1">1</a></li> <li><a href="/wiki/METAP2" title="METAP2">2</a></li></ul></li> <li><a href="/wiki/C9orf3" title="C9orf3">O</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.13_Dipeptidases" title="List of EC numbers (EC 3)">3.4.13</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Dipeptidase" title="Dipeptidase">Dipeptidase</a> <ul><li><a href="/wiki/Dipeptidase_1" title="Dipeptidase 1">1</a></li> <li><a href="/wiki/DPEP2" class="mw-redirect" title="DPEP2">2</a></li> <li><a href="/wiki/DPEP3" class="mw-redirect" title="DPEP3">3</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.14_Dipeptidyl_peptidases_and_tripeptidyl_peptidases" title="List of EC numbers (EC 3)">3.4.14</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Dipeptidyl_peptidase" title="Dipeptidyl peptidase">Dipeptidyl peptidase</a> <ul><li><a href="/wiki/Cathepsin_C" title="Cathepsin C">Cathepsin C</a></li> <li><a href="/wiki/Dipeptidyl_peptidase-4" title="Dipeptidyl peptidase-4">Dipeptidyl peptidase-4</a></li></ul></li> <li><a href="/wiki/Tripeptidyl_peptidase" title="Tripeptidyl peptidase">Tripeptidyl peptidase</a> <ul><li><a href="/wiki/Tripeptidyl_peptidase_I" title="Tripeptidyl peptidase I">Tripeptidyl peptidase I</a></li> <li><a href="/wiki/Tripeptidyl_peptidase_II" title="Tripeptidyl peptidase II">Tripeptidyl peptidase II</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.15_Peptidyl_dipeptidases" title="List of EC numbers (EC 3)">3.4.15</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Angiotensin-converting_enzyme" title="Angiotensin-converting enzyme">Angiotensin-converting enzyme</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.16_Serine_type_carboxypeptidases" title="List of EC numbers (EC 3)">3.4.16</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Serine_type_carboxypeptidase" class="mw-redirect" title="Serine type carboxypeptidase">Serine type carboxypeptidases</a>: <a href="/wiki/Cathepsin_A" title="Cathepsin A">Cathepsin A</a></li> <li><a class="mw-selflink selflink"><small>DD</small>-Transpeptidase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.17_Metallocarboxypeptidases" title="List of EC numbers (EC 3)">3.4.17</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <dl><dt><span class="nobold"><a href="/wiki/Metalloexopeptidase" title="Metalloexopeptidase">Metalloexopeptidases</a></span></dt> <dd><a href="/wiki/Carboxypeptidase" title="Carboxypeptidase">Carboxypeptidase</a> <dl><dd><a href="/wiki/Carboxypeptidase_A" title="Carboxypeptidase A">A</a></dd> <dd><a href="/wiki/Carboxypeptidase_A2" title="Carboxypeptidase A2">A2</a></dd> <dd><a href="/wiki/Carboxypeptidase_B" title="Carboxypeptidase B">B</a></dd> <dd><a href="/wiki/Cathepsin_A" title="Cathepsin A">C</a></dd> <dd><a href="/wiki/Carboxypeptidase_E" title="Carboxypeptidase E">E</a></dd> <dd><a href="/wiki/Glutamate_carboxypeptidase_II" title="Glutamate carboxypeptidase II">Glutamate II</a></dd></dl></dd></dl> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other/ungrouped</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Metalloexopeptidase" title="Metalloexopeptidase">Metalloexopeptidase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.21:_Serine_proteases" title="List of EC numbers (EC 3)">3.4.21</a>-25: <a href="/wiki/Endopeptidase" title="Endopeptidase">Endopeptidase</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Serine_protease" title="Serine protease">Serine protease</a></li> <li><a href="/wiki/Cysteine_protease" title="Cysteine protease">Cysteine protease</a></li> <li><a href="/wiki/Aspartate_protease" class="mw-redirect" title="Aspartate protease">Aspartic acid protease</a></li> <li><a href="/wiki/Metalloendopeptidase" title="Metalloendopeptidase">Metalloendopeptidase</a></li> <li><a href="/wiki/Threonine_endopeptidase" class="mw-redirect" title="Threonine endopeptidase">Threonine endopeptidase</a> <ul><li><a href="/wiki/Proteasome_endopeptidase_complex" title="Proteasome endopeptidase complex">Proteasome endopeptidase complex</a></li> <li><a href="/wiki/HslU%E2%80%94HslV_peptidase" class="mw-redirect" title="HslU—HslV peptidase">HslU—HslV peptidase</a></li></ul></li></ul> <ul><li>Other/ungrouped: <a href="/wiki/Amyloid_precursor_protein_secretase" class="mw-redirect" title="Amyloid precursor protein secretase">Amyloid precursor protein secretase</a> <ul><li><a href="/wiki/Alpha_secretase" title="Alpha secretase">Alpha secretase</a></li> <li><a href="/wiki/Beta-secretase_1" title="Beta-secretase 1">Beta-secretase 1</a></li> <li><a href="/wiki/Beta-secretase_2" title="Beta-secretase 2">Beta-secretase 2</a></li> <li><a href="/wiki/Gamma_secretase" title="Gamma secretase">Gamma secretase</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.99_Endopeptidases_of_unknown_catalytic_mechanism" title="List of EC numbers (EC 3)">3.4.99</a>: Unknown</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Staphylokinase" title="Staphylokinase">Staphylokinase</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Enzymes" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Enzymes" title="Template:Enzymes"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Enzymes" title="Template talk:Enzymes"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Enzymes" title="Special:EditPage/Template:Enzymes"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Enzymes" style="font-size:114%;margin:0 4em"><a href="/wiki/Enzyme" title="Enzyme">Enzymes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Activity</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Active_site" title="Active site">Active site</a></li> <li><a href="/wiki/Binding_site" title="Binding site">Binding site</a></li> <li><a href="/wiki/Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li> <li><a href="/wiki/Oxyanion_hole" title="Oxyanion hole">Oxyanion hole</a></li> <li><a href="/wiki/Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li> <li><a href="/wiki/Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li> <li><a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li> <li><a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Allosteric_regulation" title="Allosteric regulation">Allosteric regulation</a></li> <li><a href="/wiki/Cooperativity" title="Cooperativity">Cooperativity</a></li> <li><a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">Enzyme inhibitor</a></li> <li><a href="/wiki/Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li> <li><a href="/wiki/Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li> <li><a href="/wiki/Protein_family" title="Protein family">Enzyme family</a></li> <li><a href="/wiki/List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li> <li><a href="/wiki/Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li> <li><a href="/wiki/Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li> <li><a href="/wiki/Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li> <li><a href="/wiki/Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><b>EC1 <a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li> <li><b>EC2 <a href="/wiki/Transferase" title="Transferase">Transferases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li> <li><b>EC3 <a href="/wiki/Hydrolase" title="Hydrolase">Hydrolases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li> <li><b>EC4 <a href="/wiki/Lyase" title="Lyase">Lyases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li> <li><b>EC5 <a href="/wiki/Isomerase" title="Isomerase">Isomerases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li> <li><b>EC6 <a href="/wiki/Ligase" title="Ligase">Ligases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li> 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