Purification and primary structure of pyruvate decarboxylase from Zymomonas mobilis.
Pyruvate decarboxylase (E.C. 4.1.1.1), the key enzyme in the glycolytic pathway to ethanol, was isolated in gram amounts from Zymomonas mobilis for structural studies. The primary structure was determined by automated Edman degradation and compared with that deduced from the DNA sequence of the structural gene, previously published by two groups (A. D. Neale, R. K. Scopes, R. E. H. Wettenhall, and N. J. Hoogenraad, 1987, Nucleic Acids Res. 15, 1753-1761; M. Reynen, and H. Sahm, 1988, J. Bacteriol. 170, 3310-3313). The peptide data differ from the published DNA sequences, which also deviate from each other. Crystals diffracting to about 0.3 nm resolution have been obtained by the hanging drop vapor diffusion method. The space group was identified as P4(1)22 or its enantiomorphs containing presumably one tetramer per asymmetric unit.
Miczka
G
G
Institut für Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Jülich, Germany.
Vernau
J
J
Kula
M R
MR
Hofmann
B
B
Schomburg
D
D
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D006092:Gram-Negative Facultatively Anaerobic Rods / Q000201:enzymology*; D008969:Molecular Sequence Data; D011767:Pyruvate Decarboxylase / Q000737:chemistry / Q000302:isolation & purification*; D014462:Ultrafiltration; D014961:X-Ray Diffraction
D000596:Amino Acids; D010450:Endopeptidases; D011767:Pyruvate Decarboxylase