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Article: J1 acylase, a glutaryl-7-aminocephalosporanic acid acylase from Bacillus laterosporus J1, is a member of the α/β-hydrolase fold superfamily

TitleJ1 acylase, a glutaryl-7-aminocephalosporanic acid acylase from Bacillus laterosporus J1, is a member of the α/β-hydrolase fold superfamily
Authors
KeywordsSpecies Index: Acetobacter
Acetobacter Pasteurianus
Bacillus (Bacterium)
Bacteria (Microorganisms)
Brevibacillus Laterosporus
Rhodococcus
Rhodococcus Sp.
Issue Date2006
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2006, v. 580 n. 5, p. 1465-1471 How to Cite?
AbstractJ1 acylase, a glutaryl-7-aminocephalosporanic acid acylase (GCA) isolated from Bacillus laterosporus J1, has been conventionally grouped as the only member of class V GCA, although its amino acid sequence shares less than 10% identity with members of other classes of GCA. Instead, it shows higher sequence similarities with Rhodococcus sp. strain MB1 cocaine esterase (RhCocE) and Acetobacter turbidans α-amino acid ester hydrolase (AtAEH), members of the α/β-hydrolase fold superfamily. Homology modeling and secondary structure prediction indicate that the N-terminal region of J1 acylase has an α/β-hydrolase folding pattern. The catalytic triads in RhCocE and AtAEH were identified in J1 acylase as S125, D264 and H309. Mutations to alanine at these positions were found to completely inactivate the enzyme. These results suggest that J1 acylase is a member of the α/β-hydrolase fold superfamily with a serine-histidine-aspartate catalytic triad. © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/90622
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYau, MHen_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorTsang, PWKen_HK
dc.contributor.authorFong, WPen_HK
dc.date.accessioned2010-09-17T10:05:49Z-
dc.date.available2010-09-17T10:05:49Z-
dc.date.issued2006en_HK
dc.identifier.citationFebs Letters, 2006, v. 580 n. 5, p. 1465-1471en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90622-
dc.description.abstractJ1 acylase, a glutaryl-7-aminocephalosporanic acid acylase (GCA) isolated from Bacillus laterosporus J1, has been conventionally grouped as the only member of class V GCA, although its amino acid sequence shares less than 10% identity with members of other classes of GCA. Instead, it shows higher sequence similarities with Rhodococcus sp. strain MB1 cocaine esterase (RhCocE) and Acetobacter turbidans α-amino acid ester hydrolase (AtAEH), members of the α/β-hydrolase fold superfamily. Homology modeling and secondary structure prediction indicate that the N-terminal region of J1 acylase has an α/β-hydrolase folding pattern. The catalytic triads in RhCocE and AtAEH were identified in J1 acylase as S125, D264 and H309. Mutations to alanine at these positions were found to completely inactivate the enzyme. These results suggest that J1 acylase is a member of the α/β-hydrolase fold superfamily with a serine-histidine-aspartate catalytic triad. © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.subjectSpecies Index: Acetobacteren_HK
dc.subjectAcetobacter Pasteurianusen_HK
dc.subjectBacillus (Bacterium)en_HK
dc.subjectBacteria (Microorganisms)en_HK
dc.subjectBrevibacillus Laterosporusen_HK
dc.subjectRhodococcusen_HK
dc.subjectRhodococcus Sp.en_HK
dc.subject.meshAmidohydrolases - chemistry - genetics - metabolismen_HK
dc.subject.meshBacillus - enzymologyen_HK
dc.subject.meshBacterial Proteins - chemistryen_HK
dc.subject.meshBase Sequenceen_HK
dc.subject.meshHydrolases - chemistryen_HK
dc.subject.meshKineticsen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshProtein Conformationen_HK
dc.subject.meshProtein Structure, Secondaryen_HK
dc.subject.meshSequence Alignmenten_HK
dc.titleJ1 acylase, a glutaryl-7-aminocephalosporanic acid acylase from Bacillus laterosporus J1, is a member of the α/β-hydrolase fold superfamilyen_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.febslet.2006.01.069en_HK
dc.identifier.pmid16469317-
dc.identifier.scopuseid_2-s2.0-32344434916en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-32344434916&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume580en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1465en_HK
dc.identifier.epage1471en_HK
dc.identifier.isiWOS:000235597700042-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridYau, MH=7006864960en_HK
dc.identifier.scopusauthoridWang, J=9637013000en_HK
dc.identifier.scopusauthoridTsang, PWK=8334953500en_HK
dc.identifier.scopusauthoridFong, WP=7102816006en_HK

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