1CEV

ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6

Summary for 1CEV

• Entry DOI: 10.2210/pdb1cev/pdb
• Descriptor: PROTEIN (ARGINASE), MANGANESE (II) ION (2 entities in total)
• Functional Keywords: enzyme, hydrolase, arginine hydrolysis, nitrogen metabolism, manganese metalloenzyme
• Biological source: Bacillus caldovelox
• Total number of polymer chains: 6
• Total formula weight: 195516.74

Authors

Bewley, M.C.,Jeffrey, P.D.,Patchett, M.L.,Kanyo, Z.F.,Baker, E.N. (deposition date: 1999-03-12, release date: 1999-04-16, Last modification date: 2024-04-03)

Primary citation

Bewley, M.C.,Jeffrey, P.D.,Patchett, M.L.,Kanyo, Z.F.,Baker, E.N.
Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily.
Structure Fold.Des., 7:435-448, 1999

PubMed Abstract: Arginase is a manganese-dependent enzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. In ureotelic animals arginase is the final enzyme of the urea cycle, but in many species it has a wider role controlling the use of arginine for other metabolic purposes, including the production of creatine, polyamines, proline and nitric oxide. Arginase activity is regulated by various small molecules, including the product L-ornithine. The aim of these structural studies was to test aspects of the catalytic mechanism and to investigate the structural basis of arginase inhibition.

PubMed: 10196128
DOI: 10.1016/S0969-2126(99)80056-2

Experimental method

X-RAY DIFFRACTION (2.4 Å)