Substrate activation of brewers' yeast pyruvate decarboxylase is abolished by mutation of cysteine 221 to serine.

doi:10.1021/bi00184a035

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Article

Substrate activation of brewers' yeast pyruvate decarboxylase is abolished by mutation of cysteine 221 to serine.

Biochemistry - 10 May 1994

Baburina I, Gao Y, Hu Z, Jordan F, Hohmann S, Furey W

Abstract excerpt

Brewers' yeast pyruvate decarboxylase (EC 4.1.1.1), a thiamin diphosphate and Mg(II)-dependent enzyme, isolated from Saccharomyces cerevisiae possesses four cysteines/subunit at positions 69, 152, 221, and 222. Earlier studies conducted on a variant of the enzyme with a single Cys at position 221...

Topics

Base Sequence
Binding Sites
Cysteine
DNA Primers
Enzyme Activation
Escherichia coli
Kinetics
Molecular Sequence Data
Mutation
Pyruvate Decarboxylase
Recombinant Proteins
Saccharomyces cerevisiae
Serine
Substrate Specificity

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