Title : Role of cysteines in the activation and inactivation of brewers' yeast pyruvate decarboxylase investigated with a PDC1-PDC6 fusion protein.

Pub. Date : 1993 Mar 16

PMID : 8448127






4 Functional Relationships(s)
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1 Role of cysteines in the activation and inactivation of brewers" yeast pyruvate decarboxylase investigated with a PDC1-PDC6 fusion protein. Cysteine indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C
2 Possible roles of the Cys side chains in the activation and inactivation mechanisms of brewers" yeast pyruvate decarboxylase were investigated by comparing the behavior of the tetrameric enzyme pdc1 containing four cysteines/subunit (positions 69, 152, 221, and 222) with that of a fusion enzyme (pdc1-6, a result of spontaneous gene fusion between PDC1 and PDC6 genes) that is 84% identical in sequence with pdc1 and has only Cys221 (the other three Cys being replaced by aliphatic side chains). Cysteine indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C
3 Exposure of the fusion enzyme, just as of pdc1, to (E)-2-oxo-4-phenyl-3-butenoic acid type inhibitors/alternate substrates enabled detection of the enzyme-bound enamine intermediate at 440 nm. (E)-2-oxo-4-phenylbut-3-enoic acid indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C
4 Exposure of the fusion enzyme, just as of pdc1, to (E)-2-oxo-4-phenyl-3-butenoic acid type inhibitors/alternate substrates enabled detection of the enzyme-bound enamine intermediate at 440 nm. cyclopentyl enamine indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C