Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme.
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.
Candy
J M
JM
Centre for Protein Structure, Function and Engineering, Department of Biochemistry, University of Queensland, Brisbane 4072, Australia.
Duggleby
R G
RG
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011767:Pyruvate Decarboxylase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019289:Pyruvic Acid / Q000378:metabolism; D013835:Thiamine Pyrophosphate / Q000737:chemistry / Q000378:metabolism; D017355:Zymomonas / Q000201:enzymology*
D019289:Pyruvic Acid; D011767:Pyruvate Decarboxylase; D013835:Thiamine Pyrophosphate