Comparative characterisation of thiamin diphosphate-dependent decarboxylases
Comparative characterisation of thiamin diphosphate-dependent decarboxylases
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DOI：
10.1016/j.molcatb.2009.03.019
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发表时间：
2009-11-01
影响因子：
--
通讯作者：
Pohl, Martina
中科院分区：
文献类型：
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作者：
Gocke, Doerte;Graf, Thorsten;Pohl, Martina
几种2-酮酸脱羧酶除了其生理脱羧酶活性外，还能催化类似丙环蛋白缩合的碳糖酶反应。虽然有许多关于这些酶的稳定性和催化潜力的数据，但在类似的反应条件下缺乏标准的评价。在这项全面的调查中，我们收集了已经发表的数据，并结合了三种细菌丙酮酸脱羧酶的新研究，酵母丙酮酸脱羧酶，恶臭假单胞菌（BFD）的苯甲酰甲酸脱羧酶和乳酸乳球菌（KdcA）的支链2-酮酸脱羧酶。所得结果证明，在相同的反应条件下，活性和稳定性的最优值是相当相似的。虽然各种丙酮酸脱羧酶的脱羧酶反应底物范围相似，但与BFD和KdcA的脱羧酶反应底物范围有显著差异。我们进一步表明，从脱羧酶反应的底物范围可以可靠地预测相应酶的碳糖酶反应的可接受的供体醛的范围。(C) 2009 Elsevier B.V.版权所有
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.