Comparative characterisation of thiamin diphosphate-dependent decarboxylases

被引：43

作者：

Gocke, Doerte ^{[1
]}

Graf, Thorsten ^{[1
]}

Brosi, Helen ^{[1
]}

Frindi-Wosch, Ilona ^{[1
]}

Walter, Lydia ^{[2
]}

Mueller, Michael ^{[2
]}

Pohl, Martina ^{[1
]}

机构：

[1] Univ Dusseldorf, Res Ctr Julich, Inst Mol Enzyme Technol, D-52426 Julich, Germany

[2] Univ Freiburg, Inst Pharmaceut Sci, D-79104 Freiburg, Germany

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2009年 / 61卷 / 1-2期

关键词：

Enzymatic decarboxylation; Enzymatic carboligation; 2-Hydroxy ketones; Phenylacetylcarbinol; Acetoin; KETO ACID DECARBOXYLASE; C BOND FORMATION; PYRUVATE DECARBOXYLASE; ZYMOMONAS-MOBILIS; BENZOYLFORMATE DECARBOXYLASE; BENZALDEHYDE LYASE; ENANTIOSELECTIVE SYNTHESIS; SUBSTRATE-SPECIFICITY; ENZYMATIC-REACTIONS; PSEUDOMONAS-PUTIDA;

D O I：

10.1016/j.molcatb.2009.03.019

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Several 2-keto acid decarboxylases catalyse an acyloin condensation-like carboligase reaction beside their physiological decarboxylase activity. Although many data concerning stability and catalytic potential of these enzymes are available, a standard evaluation under similar reaction conditions is lacking. In this comprehensive survey we assemble already published data combined with new studies of three bacterial pyruvate decarboxylases, yeast pyruvate decarboxylase, benzoylformate decarboxylase from Pseudomonas putida (BFD) and the branched-chain 2-keto acid decarboxylase from Lactococcus lactis (KdcA). The obtained results proof that the optima for activity and stability are rather similar if comparable reaction conditions are used. Although the substrate ranges of the decarboxylase reaction of the various pyruvate decarboxylases are similar as well, they differ remarkably from those of BFD and KdcA. We further show that the range of acceptable donor aldehydes for the carboligase reaction of a respective enzyme can be reliably predicted from the substrate range of decarboxylase reaction. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：30 / 35

页数：6

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