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No metal cofactor in orotidine 5'-monophosphate decarboxylase
W Cui1, J G DeWitt, S M Miller
1Department of Chemistry and Biochemistry, San Francisco State University, San Francisco, California, 94132, USA.
Biochemical and Biophysical Research Communications
|May 21, 1999
Abstract:
Orotidine 5'-monophosphate decarboxylase (OMP decarboxylase, ODCase) is an important enzyme that catalyzes the final step of de novo pyrimidine nucleotide biosynthesis. The mechanism of this unique enzyme and whether metal ions play any role in catalysis have been topics of intense research interest. In this report, the role of Zn in ODCase was reexamined. Atomic absorption (AA) and X-ray absorption (XAS) spectroscopic studies did not detect zinc in active enzyme samples at high concentration. The XAS results also indicated the absence of other transition metal ions in ODCase.