Jm. Candy et Rg. Duggleby, STRUCTURE AND PROPERTIES OF PYRUVATE DECARBOXYLASE AND SITE-DIRECTED MUTAGENESIS OF THE ZYMOMONAS-MOBILIS ENZYME, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1385(2), 1998, pp. 323-338
Pyruvate decarboxylase (EC 4.1.1.1) is a thiamin diphosphate-dependent
enzyme that catalyzes the penultimate step in alcohol fermentation, T
he enzyme is widely distributed in plants and fungi but is rare in pro
karyotes and absent in animals, Here we review its structure and prope
rties with particular emphasis on how site-directed mutagenesis of the
enzyme from Zymomonas mobilis has assisted us to understand the funct
ion of critical residues, (C) 1998 Elsevier Science B.V. All rights re
served.