[Inactivation of yeast pyruvate decarboxylase in the presence of substrate and quinone electron acceptors].
The rate constants of paracatalytic inactivation of pyruvate decarboxylase in the presence of 1,4-naphthoquinones and 1,4-benzoquinones are determined by redox potentials of the oxidant. The logarithm of k2 depends hyperbolically on the redox potential of quinone E0(Q/Q-.) with the coefficient of proportionality which approximates 8.4, The absence of considerable deviations in this correlation for the oxidants of different structures with closed values Eo(Q/Q-.) indicates that the enzyme produces no additional steric barrier.
Vovk
A I
AI
Parkhomenko
Iu M
IuM
Murav'eva
I V
IV
Protasova
Z S
ZS
D016227:Benzoquinones / Q000378:metabolism* / Q000494:pharmacology; D002384:Catalysis / Q000187:drug effects; D003653:Decarboxylation / Q000187:drug effects; D004579:Electron Transport / Q000187:drug effects; D007700:Kinetics; D009285:Naphthoquinones / Q000494:pharmacology; D010084:Oxidation-Reduction / Q000187:drug effects; D011767:Pyruvate Decarboxylase / Q000037:antagonists & inhibitors* / Q000187:drug effects / Q000302:isolation & purification; D013379:Substrate Specificity / Q000187:drug effects; D015003:Yeasts / Q000187:drug effects / Q000201:enzymology*
D016227:Benzoquinones; D009285:Naphthoquinones; C004532:quinone; D011767:Pyruvate Decarboxylase