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All but one of Biochemistry, University 38 enzyme variants examined were thermally stable and had native-like Walk, Bristol, BS8 1TD, UK hydrodynamic properties. In this sample, there was no bias detected in either the DNA or amino acid sequences encoded. We argue that the a E -b D surface loop sequence is unimportant for protein folding or stability and can be fully varied to select enzymes with new substrate specificities. The selection of NAD-dependent dehydrogenases with specificity for: malate, phenyllactate, hydroxyisocaproate and 4-phenyl-2-hydroxybutanoate from two bsLDH libraries is described. This required a highly discriminatory screen for 2-hydroxy acid dehydrogenase activity to select enzymes which, in the absence of the natural allosteric activator fructose-1,6-bisphosphate (FBP), maintained high temperature stability and catalytic activity without substrate inhibition.","publication_date":"1996,,","publication_name":"Journal of Molecular Biology","grobid_abstract_attachment_id":"41816432"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":"high","language":"en","title":"Guided Evolution of Enzymes with New Substrate Specificities","broadcastable":true,"draft":null,"has_indexable_attachment":true,"indexable":true}}["work"]; window.loswp.workCoauthors = [14775645]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "ds_vanilla"; window.loswp.fullPageMobileSutdModalVariant = "full_page_mobile_sutd_modal"; window.loswp.useOptimizedScribd4genScript = false; window.loswp.appleClientId = 'edu.academia.applesignon';</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="ds-loswp-container"><div class="ds-work-card--grid-container"><div class="ds-work-card--container js-loswp-work-card"><div class="ds-work-card--cover"><div class="ds-work-cover--wrapper"><div class="ds-work-cover--container"><button class="ds-work-cover--clickable js-swp-download-button" data-signup-modal="{"location":"swp-splash-paper-cover","attachmentId":41816432,"attachmentType":"pdf"}"><img alt="First page of “Guided Evolution of Enzymes with New Substrate Specificities”" class="ds-work-cover--cover-thumbnail" src="https://0.academia-photos.com/attachment_thumbnails/41816432/mini_magick20190218-3389-1kjvoog.png?1550529255" /><img alt="PDF Icon" class="ds-work-cover--file-icon" src="//a.academia-assets.com/assets/single_work_splash/adobe.icon-574afd46eb6b03a77a153a647fb47e30546f9215c0ee6a25df597a779717f9ef.svg" /><div class="ds-work-cover--hover-container"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span><p>Download Free PDF</p></div><div class="ds-work-cover--ribbon-container">Download Free PDF</div><div class="ds-work-cover--ribbon-triangle"></div></button></div></div></div><div class="ds-work-card--work-information"><h1 class="ds-work-card--work-title">Guided Evolution of Enzymes with New Substrate Specificities</h1><div class="ds-work-card--work-authors ds-work-card--detail"><a class="ds-work-card--author js-wsj-grid-card-author ds2-5-body-md ds2-5-body-link" data-author-id="14775645" href="https://bristol.academia.edu/RichardSessions"><img alt="Profile image of Richard Sessions" class="ds-work-card--author-avatar" src="//a.academia-assets.com/images/s65_no_pic.png" />Richard Sessions</a></div><div class="ds-work-card--detail"><p class="ds-work-card--detail ds2-5-body-sm">1996, Journal of Molecular Biology</p><div class="ds-work-card--work-metadata"><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">visibility</span><p class="ds2-5-body-sm" id="work-metadata-view-count">…</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">description</span><p class="ds2-5-body-sm">14 pages</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">link</span><p class="ds2-5-body-sm">1 file</p></div></div><script>(async () => { const workId = 21324568; 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class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="14775645" href="https://bristol.academia.edu/RichardSessions">Richard Sessions</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Protein Engineering Design and Selection, 1999</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"A general method for relieving substrate inhibition in lactate dehydrogenases","attachmentId":41816420,"attachmentType":"pdf","work_url":"https://www.academia.edu/21324584/A_general_method_for_relieving_substrate_inhibition_in_lactate_dehydrogenases","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/21324584/A_general_method_for_relieving_substrate_inhibition_in_lactate_dehydrogenases"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="7" data-entity-id="117085635" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/117085635/Alteration_of_Substrate_Specificity_of_Leucine_Dehydrogenase_by">Alteration of Substrate Specificity of Leucine Dehydrogenase by</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="113726097" href="https://kanazawa-u.academia.edu/KunishigeKATAOKA">Kunishige KATAOKA</a></div><p class="ds-related-work--metadata ds2-5-body-xs">2014</p><p class="ds-related-work--abstract ds2-5-body-sm">The residues L40, A113, V291, and V294, in leucine dehydrogenase (LeuDH), predicted to be involved in recognition of the substrate side chain, have been mutated on the basis of the molecular modeling to mimic the substrate specificities of phenylalanine (PheDH), glutamate (GluDH), and lysine dehydrogenases (LysDH). The A113G and A113G/V291L mutants, imitating the PheDH active site, displayed activities toward L-phenylalanine and phenylpyruvate with 1.6 and 7.8 % of kcat values of the wild-type enzyme for the preferred substrates, L-leucine and its keto-analog, respectively. Indeed, the residue A113, corresponding to G114 in PheDH, affects the volume of the side-chain binding pocket and has a critical role in discrimination of the bulkiness of the side chain. Another two sets of mutants, substituting L40 and V294 of LeuDH with the corresponding residues predicted in GluDH and LysDH, were also constructed and characterized. Emergence of GluDH and LysDH activities in L40K/V294S and L40...</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Alteration of Substrate Specificity of Leucine Dehydrogenase by","attachmentId":113038182,"attachmentType":"pdf","work_url":"https://www.academia.edu/117085635/Alteration_of_Substrate_Specificity_of_Leucine_Dehydrogenase_by","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/117085635/Alteration_of_Substrate_Specificity_of_Leucine_Dehydrogenase_by"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" 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CHEMICAL MODIFICATION WITH 2,4,6-TRINITROBENZENESULFONIC ACID, N-SUCCINIMIDYL 3-(2-PYRIDYLDITHIO)PROPIONATE, AND 5prime -(P-(FLUOROSULFONYL)BENZOYL)ADENOSINE</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="38003324" href="https://sjmch.academia.edu/JoseRemacle">Jose Remacle</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Biological Chemistry, 1997</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Identification of Lysine 74in the Pyruvate Binding Site of Alanine Dehydrogenase from Bacillus subtilis. CHEMICAL MODIFICATION WITH 2,4,6-TRINITROBENZENESULFONIC ACID, N-SUCCINIMIDYL 3-(2-PYRIDYLDITHIO)PROPIONATE, AND 5prime -(P-(FLUOROSULFONYL)BENZOYL)ADENOSINE","attachmentId":73966318,"attachmentType":"pdf","work_url":"https://www.academia.edu/60590329/Identification_of_Lysine_74in_the_Pyruvate_Binding_Site_of_Alanine_Dehydrogenase_from_Bacillus_subtilis_CHEMICAL_MODIFICATION_WITH_2_4_6_TRINITROBENZENESULFONIC_ACID_N_SUCCINIMIDYL_3_2_PYRIDYLDITHIO_PROPIONATE_AND_5prime_P_FLUOROSULFONYL_BENZOYL_ADENOSINE","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/60590329/Identification_of_Lysine_74in_the_Pyruvate_Binding_Site_of_Alanine_Dehydrogenase_from_Bacillus_subtilis_CHEMICAL_MODIFICATION_WITH_2_4_6_TRINITROBENZENESULFONIC_ACID_N_SUCCINIMIDYL_3_2_PYRIDYLDITHIO_PROPIONATE_AND_5prime_P_FLUOROSULFONYL_BENZOYL_ADENOSINE"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="22" data-entity-id="58437039" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/58437039/Refined_crystal_structure_of_cytoplasmic_malate_dehydrogenase_at_2_5_ANG_resolution">Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-.ANG. resolution</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="41272296" href="https://independent.academia.edu/JensBirktoft">Jens Birktoft</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biochemistry, 1989</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-.ANG. resolution","attachmentId":72848835,"attachmentType":"pdf","work_url":"https://www.academia.edu/58437039/Refined_crystal_structure_of_cytoplasmic_malate_dehydrogenase_at_2_5_ANG_resolution","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/58437039/Refined_crystal_structure_of_cytoplasmic_malate_dehydrogenase_at_2_5_ANG_resolution"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="23" data-entity-id="25377581" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/25377581/Deletion_variants_of_l_hydroxyisocaproate_dehydrogenase_Probing_substrate_specificity">Deletion variants of l-hydroxyisocaproate dehydrogenase. 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