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.
Uridine phosphorylase from Escherichia coli B. Enzymatic and molecular properties / Vita, A.; Amici, Adolfo; Cacciamani, Tiziana; Lanciotti, M.; Magni, Giulio. - In: INTERNATIONAL JOURNAL OF BIOCHEMISTRY. - ISSN 0020-711X. - STAMPA. - 18:5(1986), pp. 431-436. [10.1016/0020-711X(86)90185-0]
Uridine phosphorylase from Escherichia coli B. Enzymatic and molecular properties.
AMICI, Adolfo;CACCIAMANI, Tiziana;MAGNI, GIULIO
1986-01-01
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
