STRUCTURE AND PROPERTIES OF PYRUVATE DECARBOXYLASE AND SITE-DIRECTED MUTAGENESIS OF THE ZYMOMONAS-MOBILIS ENZYME

Citation
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
Citations number
126
Categorie Soggetti
Biology,Biophysics
ISSN journal
01674838
Volume
1385
Issue
2
Year of publication
1998
Pages
323 - 338
Database
ISI
SICI code
0167-4838(1998)1385:2<323:SAPOPD>2.0.ZU;2-2
Abstract
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.