User:Joseph Whaley/Sandbox 650
From Proteopedia
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Introduction
Arginase belongs to the hydrolase family and is typically in the alpha-beta-alpha structure. The proteins associated with the hydrolase family play important roles in arginine metabolism, the urea cycle, and histidine degradation. This enzyme can be deficient in some organisms. Arginase deficiency is hereditary and rare. If arginase is missing, arginine is not broken down properly and urea cannot be produced; thus, nitrogen accumulates in the blood in the form of ammonia ultimately causing neurological and developmental issues. Arginase is the fifth and final enzyme used in the Urea Cycle to produce ornithine from arginine and exert ammonia as a biproduct. In order for arginase to to produce ornithine, the active site of arginine must be bound by a metal ion in order to facilitate hydrogen-bonding-assisted stability of the substrate. The enzyme demonstrates a highly specific active site allowing for a conserved structural arrangement allowing for the hydrolysis of arginine to form ornithine.
Structure and Functionality
References
^ MeSH Ureohydrolases ^ a b Lee J, Suh SW, Kim KH, Kim D, Yoon HJ, Kwon AR, Ahn HJ, Ha JY, Lee HH (2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily". J. Biol. Chem. 279 (48): -. doi:10.1074/jbc.M409246200. PMID 15355972. ^ Christianson DW, Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F (2005). "Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response". Proc. Natl. Acad. Sci. U.S.A. 102 (37): -. doi:10.1073/pnas.0504027102. PMC 1201588. PMID 16141327. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1201588.
