کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
70754 48845 2009 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Comparative characterisation of thiamin diphosphate-dependent decarboxylases
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
پیش نمایش صفحه اول مقاله
Comparative characterisation of thiamin diphosphate-dependent decarboxylases
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 61, Issues 1–2, November 2009, Pages 30–35
نویسندگان
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