No metal cofactor in orotidine 5 '-monophosphate decarboxylase

Citation
Wd. Cui et al., No metal cofactor in orotidine 5 '-monophosphate decarboxylase, BIOC BIOP R, 259(1), 1999, pp. 133-135
Citations number
16
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
259
Issue
1
Year of publication
1999
Pages
133 - 135
Database
ISI
SICI code
0006-291X(19990527)259:1<133:NMCIO5>2.0.ZU;2-2
Abstract
Orotidine 5'-monophosphate decarboxylase (OMP decarboxylase, ODCase) is an important enzyme that catalyzes the final step of de novo pyrimidine nucleo tide biosynthesis. The mechanism of this unique enzyme and whether metal io ns play any role in catalysis have been topics of intense research interest . In this report, the role of Zn in ODCase was reexamined. Atomic absorptio n (AA) and X-ray absorption (XAS) spectroscopic studies did not detect zinc in active enzyme samples at high concentration. The XAS results also indic ated the absence of other transition metal ions in ODCase. (C) 1999 Academi c Press.