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Biochim Biophys Acta. 1998 Jun 29;1385(2):323-38.

Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme.

Author information

1
Centre for Protein Structure, Function and Engineering, Department of Biochemistry, University of Queensland, Brisbane 4072, Australia.

Abstract

Pyruvate decarboxylase (EC 4.1.1.1) is a thiamin diphosphate-dependent enzyme that catalyzes the penultimate step in alcohol fermentation. The enzyme is widely distributed in plants and fungi but is rare in prokaryotes and absent in animals. Here we review its structure and properties with particular emphasis on how site-directed mutagenesis of the enzyme from Zymomonas mobilis has assisted us to understand the function of critical residues.

PMID:
9655927
DOI:
10.1016/s0167-4838(98)00077-6
[Indexed for MEDLINE]

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