DC FieldValueLanguage
dc.contributor.authorGeng, Feng-
dc.contributor.authorMa, Cheng-Wei-
dc.contributor.authorZeng, An-Ping-
dc.date.accessioned2019-08-30T04:59:28Z-
dc.date.available2019-08-30T04:59:28Z-
dc.date.issued2017-02-09-
dc.identifier.citationBiotechnology Letters 4 (39): 599-605 (2017-04-01)de_DE
dc.identifier.issn1573-6776de_DE
dc.identifier.urihttp://hdl.handle.net/11420/3232-
dc.description.abstractObjective: To re-engineer the active site of proteins for non-natural substrates using a position-based prediction method (PBPM). Results: The approach has been applied to re-engineer the E. coli glutamate dehydrogenase to alter its substrate from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway. After identification of key residues that determine the substrate specificity, residue K92 was selected as a candidate site for mutation. Among the three mutations (K92V, K92C, and K92M) suggested by PBPM, the specific activity of the best mutant (K92 V) was increased from 171 ± 35 to 1328 ± 71 μU mg−1. Conclusion: The PBPM approach has a high efficiency for re-engineering the substrate specificity of natural enzymes for new substrates.en
dc.language.isoende_DE
dc.publisherSpringer Science + Business Media B.Vde_DE
dc.relation.ispartofBiotechnology lettersde_DE
dc.subjectEnzyme designde_DE
dc.subjectGlutamate dehydrogenasede_DE
dc.subjectHomoserinede_DE
dc.subjectPosition-based prediction methodde_DE
dc.subject1,3-Propanediolde_DE
dc.subjectProtein engineeringde_DE
dc.subjectSubstrate specificityde_DE
dc.subject.ddc570: Biowissenschaften, Biologiede_DE
dc.subject.ddc610: Medizinde_DE
dc.titleReengineering substrate specificity of E. coli glutamate dehydrogenase using a position-based prediction methodde_DE
dc.typeArticlede_DE
dc.type.diniarticle-
dc.subject.ddccode570-
dc.subject.ddccode610-
dcterms.DCMITypeText-
tuhh.abstract.englishObjective: To re-engineer the active site of proteins for non-natural substrates using a position-based prediction method (PBPM). Results: The approach has been applied to re-engineer the E. coli glutamate dehydrogenase to alter its substrate from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway. After identification of key residues that determine the substrate specificity, residue K92 was selected as a candidate site for mutation. Among the three mutations (K92V, K92C, and K92M) suggested by PBPM, the specific activity of the best mutant (K92 V) was increased from 171 ± 35 to 1328 ± 71 μU mg−1. Conclusion: The PBPM approach has a high efficiency for re-engineering the substrate specificity of natural enzymes for new substrates.de_DE
tuhh.publisher.doi10.1007/s10529-017-2297-2-
tuhh.publication.instituteBioprozess- und Biosystemtechnik V-1de_DE
tuhh.type.opus(wissenschaftlicher) Artikel-
tuhh.institute.germanBioprozess- und Biosystemtechnik V-1de
tuhh.institute.englishBioprozess- und Biosystemtechnik V-1de_DE
tuhh.gvk.hasppnfalse-
dc.type.driverarticle-
dc.type.casraiJournal Article-
tuhh.container.issue4de_DE
tuhh.container.volume39de_DE
tuhh.container.startpage599de_DE
tuhh.container.endpage605de_DE
item.languageiso639-1en-
item.fulltextNo Fulltext-
item.openairetypeArticle-
item.grantfulltextnone-
item.creatorOrcidGeng, Feng-
item.creatorOrcidMa, Cheng-Wei-
item.creatorOrcidZeng, An-Ping-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.creatorGNDGeng, Feng-
item.creatorGNDMa, Cheng-Wei-
item.creatorGNDZeng, An-Ping-
item.cerifentitytypePublications-
crisitem.author.deptBioprozess- und Biosystemtechnik V-1-
crisitem.author.deptBioprozess- und Biosystemtechnik V-1-
crisitem.author.deptBioprozess- und Biosystemtechnik V-1-
crisitem.author.orcid0000-0001-9768-7096-
crisitem.author.parentorgStudiendekanat Verfahrenstechnik-
crisitem.author.parentorgStudiendekanat Verfahrenstechnik-
crisitem.author.parentorgStudiendekanat Verfahrenstechnik-
Appears in Collections:Publications without fulltext
Show simple item record

Page view(s)

51
Last Week
0
Last month
0
checked on Oct 20, 2020

Google ScholarTM

Check

Add Files to Item

Note about this record

Export

Items in TORE are protected by copyright, with all rights reserved, unless otherwise indicated.