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Article: A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilis d-amino acid oxidase

TitleA single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilis d-amino acid oxidase
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2010
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/713354/description#description
Citation
New Biotechnology, 2010, v. 27 n. 1, p. 78-84 How to Cite?
AbstractThe industrial importance of Trigonopsis variabilis d-amino acid oxidase (TvDAAO) is represented by its biocatalytic oxidative deamination of cephalosporin C (CPC) to yield glutaryl-7-aminocephalosporanic acid (GL-7-ACA). The process has been incorporated into a two-step bioconversion to produce 7-aminocephalosporanic acid, the crucial synthetic nucleus for several semi-synthetic cephalosporin antibiotics. A homology model of TvDAAO indicated that residue F54 is in a close proximity to the in silico docked CPC. Substitution of this F54 to Tyr (F54Y) resulted in 6-fold improvement in k cat,app and ~2.5-fold increase in K i of GL-7-ACA. Heat treatment (55°C, 60min) did not decrease the activity of F54Y. It is suggested that the Tyr substitution might initiate hydrogen bond formation with the amino group of CPC and facilitate deamination. Faster substrate turnover, reduced GL-7-ACA inhibition and improved thermostability of the F54Y substitution render it a useful candidate in industrial production of semi-synthetic cephems. © 2009 Elsevier B.V.
Persistent Identifierhttp://hdl.handle.net/10722/90626
ISSN
2015 Impact Factor: 3.199
2015 SCImago Journal Rankings: 1.092
ISI Accession Number ID
Funding AgencyGrant Number
Research Grants Council of the Hong Kong Special Administrative Region, ChinaHKU 475007M
Funding Information:

The work described in this paper was fully supported by a grant from the Research Grants Council of the Hong Kong Special Administrative Region, China (Project No. HKU 475007M). We are grateful to Dr Amanda N.S. Mak for her excellent technical assistance and to Prof. J. Wang and Dr Jimmy M.H. Yau for their support.

References
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DC FieldValueLanguage
dc.contributor.authorWong, KSen_HK
dc.contributor.authorFong, WPen_HK
dc.contributor.authorTsang, PWKen_HK
dc.date.accessioned2010-09-17T10:05:53Z-
dc.date.available2010-09-17T10:05:53Z-
dc.date.issued2010en_HK
dc.identifier.citationNew Biotechnology, 2010, v. 27 n. 1, p. 78-84en_HK
dc.identifier.issn1871-6784en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90626-
dc.description.abstractThe industrial importance of Trigonopsis variabilis d-amino acid oxidase (TvDAAO) is represented by its biocatalytic oxidative deamination of cephalosporin C (CPC) to yield glutaryl-7-aminocephalosporanic acid (GL-7-ACA). The process has been incorporated into a two-step bioconversion to produce 7-aminocephalosporanic acid, the crucial synthetic nucleus for several semi-synthetic cephalosporin antibiotics. A homology model of TvDAAO indicated that residue F54 is in a close proximity to the in silico docked CPC. Substitution of this F54 to Tyr (F54Y) resulted in 6-fold improvement in k cat,app and ~2.5-fold increase in K i of GL-7-ACA. Heat treatment (55°C, 60min) did not decrease the activity of F54Y. It is suggested that the Tyr substitution might initiate hydrogen bond formation with the amino group of CPC and facilitate deamination. Faster substrate turnover, reduced GL-7-ACA inhibition and improved thermostability of the F54Y substitution render it a useful candidate in industrial production of semi-synthetic cephems. © 2009 Elsevier B.V.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/713354/description#descriptionen_HK
dc.relation.ispartofNew Biotechnologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleA single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilis d-amino acid oxidaseen_HK
dc.typeArticleen_HK
dc.identifier.emailTsang, PWK: pwktsang@hku.hken_HK
dc.identifier.authorityTsang, PWK=rp01388en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.nbt.2009.11.002en_HK
dc.identifier.pmid19909828-
dc.identifier.scopuseid_2-s2.0-77952507592en_HK
dc.identifier.hkuros171291-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77952507592&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume27en_HK
dc.identifier.issue1en_HK
dc.identifier.spage78en_HK
dc.identifier.epage84en_HK
dc.identifier.eissn1876-4347-
dc.identifier.isiWOS:000276148500012-
dc.publisher.placeNetherlandsen_HK
dc.relation.projectCharacterization of highly active, thermostable mutants of Trigonopsis variabilis D-Amino acid oxidase for antibiotics production: Kinetic measurements, structural studies and beyond-
dc.identifier.scopusauthoridWong, KS=35191126000en_HK
dc.identifier.scopusauthoridFong, WP=7102816006en_HK
dc.identifier.scopusauthoridTsang, PWK=8334953500en_HK

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