1a9x

From Proteopedia

Revision as of 10:55, 30 October 2007

CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS

Overview

Carbamoyl phosphate synthetase from Escherichia coli catalyzes the, production of carbamoyl phosphate from two molecules of Mg2+ATP, one, molecule of bicarbonate, and one molecule of glutamine. The enzyme, consists of two polypeptide chains referred to as the large and small, subunits. While the large subunit provides the active sites responsible, for the binding of nucleotides and other effector ligands, the small, subunit contains those amino acid residues that catalyze the hydrolysis of, glutamine to glutamate and ammonia. From both amino acid sequence analyses, and structural studies it is now known that the small subunit belongs to, the class I amidotransferase family of enzymes. Numerous biochemical, studies have suggested that the reaction mechanism of the small subunit, proceeds ... [(full description)]

About this Structure

1A9X is a [Protein complex] structure of sequences from [Escherichia coli] with MN, K, PO4, CL, ADP, ORN and NET as [ligands]. Structure known Active Site: . Full crystallographic information is available from [OCA].

Reference

Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis., Thoden JB, Miran SG, Phillips JC, Howard AJ, Raushel FM, Holden HM, Biochemistry. 1998 Jun 23;37(25):8825-31. PMID:9636022

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