来自大肠杆菌B的尿苷磷酸化酶。酶学和分子特性。

Uridine phosphorylase from Escherichia coli B. Enzymatic and molecular properties.

作者信息

Vita A, Amici A, Cacciamani T, Lanciotti M, Magni G

出版信息

Int J Biochem. 1986;18(5):431-5. doi: 10.1016/0020-711x(86)90185-0.

PMID:3519310

Abstract

Uridine phosphorylase (EC 2.4.2.3) from Escherichia coli B is an oligomeric protein composed of four identical subunits of 29,000 mol. wt. The enzyme has four half-cystine residues per subunit titrable only in denaturing condition. No disulphide linkages either inter- or intra-chain are present. The isoelectric point is 5.25. The enzyme shows strict specificity toward uridine and 5-methyluridine and is inhibited by thymine, deoxycytidine and heavy metal ions.

摘要

来自大肠杆菌B的尿苷磷酸化酶（EC 2.4.2.3）是一种寡聚蛋白，由四个相同的亚基组成，每个亚基的分子量为29,000道尔顿。该酶每个亚基有四个半胱氨酸残基，只有在变性条件下才可滴定。链间或链内均不存在二硫键。其等电点为5.25。该酶对尿苷和5-甲基尿苷表现出严格的特异性，并受到胸腺嘧啶、脱氧胞苷和重金属离子的抑制。