Uridine phosphorylase from Escherichia coli B. enzymatic and molecular properties

Alberto Vita, Adolfo Amici, Tiziana Cacciamani, Marina Lanciotti, Giulio Magni

Research output: Contribution to journalArticlepeer-review

Abstract

1. 1. 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. 2. 2. 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 isolectic point is 5.25. 3. 3. The enzyme shows strict specificity toward uridine and 5-methyluridine and is inhibited by thymine, deoxycytidine and heavy metal ions.

Original languageEnglish
Pages (from-to)431-435
Number of pages5
JournalInternational Journal of Biochemistry
Volume18
Issue number5
DOIs
Publication statusPublished - 1986

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Uridine phosphorylase from Escherichia coli B. enzymatic and molecular properties'. Together they form a unique fingerprint.

Cite this