1CEV

ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6

1CEV の概要

• エントリーDOI: 10.2210/pdb1cev/pdb
• 分子名称: PROTEIN (ARGINASE), MANGANESE (II) ION (2 entities in total)
• 機能のキーワード: enzyme, hydrolase, arginine hydrolysis, nitrogen metabolism, manganese metalloenzyme
• 由来する生物種: Bacillus caldovelox
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 195516.74

構造登録者

Bewley, M.C.,Jeffrey, P.D.,Patchett, M.L.,Kanyo, Z.F.,Baker, E.N. (登録日: 1999-03-12, 公開日: 1999-04-16, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)