Linked Life Data

21207573

Source:http://linkedlifedata.com/resource/pubmed/id/21207573

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-1-5
pubmed:abstractText
Variant G74C of arylmalonate decarboxylase (AMDase) from Bordatella bronchoseptica has a unique racemising activity towards profens. By protein engineering, variant G74C/V43A with a 20-fold shift towards promiscuous racemisation was obtained, based on a reduced activity in the decarboxylation reaction and a two-fold increase in the racemisation activity. The mutant showed an extended substrate range, with a 30-fold increase in the reaction rate towards ketoprofen. Molecular dynamics simulations and the substrate profile of the racemase indicate that the steric and polar effects of the substrate structure play a more dominant role on catalysis than mere kinetic ?-proton acidity. The observation that the conversion of ?,?-unsaturated carboxylic acids does not lead to a rearrangement to form their ?,? isomers indicates a concerted rather than a stepwise mechanism. Interestingly, a substrate bearing a nitro group instead of the carboxylic acid group on the ?-carbon atom was also converted by the racemase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1521-3765
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
pubmed:issnType
Electronic
pubmed:day
10
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
557-63
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Engineering the promiscuous racemase activity of an arylmalonate decarboxylase.
pubmed:affiliation
Department of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, 2238522 Yokohama, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't