No metal cofactor in orotidine 5′-monophosphate decarboxylase

被引：33

作者：

Cui, WD

DeWitt, JG

Miller, SM

Wu, WM ^{[1
]}

机构：

[1] San Francisco State Univ, Dept Chem & Biochem, San Francisco, CA 94132 USA

[2] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 259卷 / 01期

关键词：

D O I：

10.1006/bbrc.1999.0737

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1999 Academic Press.

引用

页码：133 / 135

页数：3

共 16 条

[1] OROTIDINE-5'-MONOPHOSPHATE DECARBOXYLASE CATALYSIS - KINETIC ISOTOPE EFFECTS AND THE STATE OF HYBRIDIZATION OF A BOUND TRANSITION-STATE ANALOG [J].