Linked Life Data

8000863

Source:http://linkedlifedata.com/resource/pubmed/id/8000863

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-1-23
pubmed:abstractText
The newly described carbonyl reductase from Rhodococcus erythropolis (RECR) accepts a broad range of substrates. Based on the kinetic constants of a variety of methyl and ethyl ketones a hypothetical model of the substrate-binding site is proposed. Whether a substrate of interest may be reduced by the RECR can be predicted from this model together with the kinetic data. A study of initial velocities and product inhibition is presented, which shows that the kinetics of the RECR follow a Theorell-Chance mechanism. The pro-R hydride of NADH is transferred by the enzyme to the re face of the carbonyl compounds yielding (S)-alcohols. The reduction of methyl 3-oxobutanoate and ethyl 4-chloro-3-oxobutanoate catalyzed by the oxidoreductase lead to the corresponding hydroxy compounds with high enantiomeric purity [enantiomeric excess (e.e.) > or = 99%]. The synthesis of ethyl (2R,3S)-3-hydroxy-2-methylbutanoate was accomplished with high diastereoselectivity (diastereomeric excess = 95%) and enantioselectivity (e.e. > or = 95%).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0968-0896
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
A kinetic study and application of a novel carbonyl reductase isolated from Rhodococcus erythropolis.
pubmed:affiliation
Institut für Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich (KFA), Germany.
pubmed:publicationType
Journal Article, Comparative Study