TY - JOUR
T1 - Comparative characterisation of thiamin diphosphate-dependent decarboxylases
AU - Gocke, Dörte
AU - Graf, Thorsten
AU - Brosi, Helen
AU - Frindi-Wosch, Ilona
AU - Walter, Lydia
AU - Müller, Michael
AU - Pohl, Martina
N1 - Funding Information:
The skilful technical assistance of Katharina Range is gratefully acknowledged. The ScPDC gene was kindly provided by PD Dr. Stephan König from the Martin-Luther University Halle-Wittenberg. The authors thank Evonik Industries (formerly Degussa AG) for financial support.
PY - 2009/11
Y1 - 2009/11
N2 - 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.
AB - 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.
KW - 2-Hydroxy ketones
KW - Acetoin
KW - Enzymatic carboligation
KW - Enzymatic decarboxylation
KW - Phenylacetylcarbinol
UR - http://www.scopus.com/inward/record.url?scp=70349522120&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2009.03.019
DO - 10.1016/j.molcatb.2009.03.019
M3 - Article
AN - SCOPUS:70349522120
SN - 1381-1177
VL - 61
SP - 30
EP - 35
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
IS - 1-2
ER -