Who's Who? Allocation of Carbonyl Reductase Isoenzymes from Candida parapsilosis by Combining Bio- and Computational Chemistry

Proof of identity: The previously described ability of Candida parapsilosis lysate to reduce structurally diverse ketones led to the discovery of two carbonyl reductases as possible candidates for this interesting biotransformation. Homology modelling and prediction of indicator substrates helped to...

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Published inChembiochem : a European journal of chemical biology Vol. 13; no. 6; pp. 803 - 809
Main Authors Jakoblinnert, Andre, Bocola, Marco, Bhattacharjee, Monideepa, Steinsiek, Sonja, Bönitz-Dulat, Mara, Schwaneberg, Ulrich, Ansorge-Schumacher, Marion B.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 16.04.2012
WILEY‐VCH Verlag
Subjects
Alcohol Oxidoreductases - chemistry
Alcohol Oxidoreductases - metabolism
Aldehyde Reductase
Aldo-Keto Reductases
Amino Acid Sequence
Binding Sites
Candida - chemistry
Candida - enzymology
Candida parapsilosis
homology modeling
indicator substrate
isoenzyme assignment
Isoenzymes
ketones
Molecular Sequence Data
reduction
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Summary:Proof of identity: The previously described ability of Candida parapsilosis lysate to reduce structurally diverse ketones led to the discovery of two carbonyl reductases as possible candidates for this interesting biotransformation. Homology modelling and prediction of indicator substrates helped to identify which enzyme has the large substrate scope verified by biochemical data.
Bibliography:ark:/67375/WNG-0NJ2JCN0-X
AiF - No. 13386N/1
Deutsche Forschungsgemeinschaft - No. AN387/1; No. GRK 1166
istex:EA1C30F277B09A2438EC798C0D0FC666BAA39F8A
ArticleID:CBIC201200023
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201200023