title: No metal cofactor in orotidine 5'-monophosphate decarboxylase.
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.
authors.affiliation: Department of Chemistry and Biochemistry, San Francisco State University, San Francisco, California, 94132, USA.
authors.forename: W
authors.initials: W
authors.lastname: Cui
authors.forename: J G
authors.initials: JG
authors.lastname: DeWitt
authors.forename: S M
authors.initials: SM
authors.lastname: Miller
authors.forename: W
authors.initials: W
authors.lastname: Wu
mesh_terms: D002384:Catalysis; D015394:Molecular Structure; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000737:chemistry*; D012441:Saccharomyces cerevisiae; D013054:Spectrophotometry, Atomic; D013057:Spectrum Analysis; D015032:Zinc / Q000032:analysis*
chemical_list: D009964:Orotidine-5'-Phosphate Decarboxylase; D015032:Zinc