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Carbamoyl phosphate synthetase I
Carbamoyl Phosphate Synthetase I is a ligase enzyme located in the mitochondria involved in the production of urea. Carbamoyl Phosphate Synthetase I (CPSI) transfers an ammonia molecule from glutamine or glutamate to a molecule of bicarbonate that has been phosphorylated by a molecule of ATP. The resulting carbamate is then phosphorylated with another molecule ATP. The resulting molecule of carbamoyl phosphate leaves the enzyme.
==Structure of Carbamoyl Phosphate Synthetase I==
CPSI is a heterodimer with a small subunit and a larger subunit with about 382 and 1073 amino acid residues in size.〔James B. Thoden‡, Xinyi Hua, et al. “Carbamoyl-phosphate Synthetase: Creation of an Escape Route for Ammonia.” From the ‡Department of Biochemistry, University of Wisconsin, Madison, Wisconsin, 53706-1544 and the §Department of Chemistry, Texas A&M University, College Station, Texas 77843-3012. http://www.jbc.org/cgi/reprint/277/42/39722.pdf〕 The small subunit contains one active site for the binding and deamination of glutamine to make ammonia and glutamate. The large subunit contains two active sites, one for the production of carboxyphosphate, and the other for the production of carbamoyl phosphate.〔SUE GLENN POWERS, “Inhibition of Carbamyl Phosphate Synthetase by PI, P5-Di (adenosine 5’) - pentaphosphate EVIDENCE FOR TWO ATP BINDING SITES.” From the Department ofBiochemistry, Cornell University Medical College, New York, New York 10021. http://www.jbc.org/cgi/reprint/252/10/3558〕〔James B. Thoden, Hazel M. Holden, et al. (1997). “Structure of Carbamoyl Phosphate Synthetase: A Journey of 96 Å from Substrate to Product.” Institute for Enzyme Research, Graduate School, and Department of Biochemistry, College of Agriculture, UniVersity of Wisconsin, Madison, Wisconsin 53705, and Department of Chemistry, Texas A&M UniVersity, College Station, Texas 77843. http://pubs.acs.org/cgi-bin/article.cgi/bichaw/1997/36/i21/pdf/bi970503q.pdf〕 Within the large subunit there are two domains (B and C) each with an active site of the ATP-grasp family.〔 Connecting the two subunits is a tunnel of sorts, which directs the ammonia from the small subunit to the large subunit.〔Jungwook Kim and Frank M. Raushel (2004). “Perforation of the Tunnel Wall in Carbamoyl Phosphate Synthetase Derails the Passage of Ammonia between Sequential Active Sites.” Department of Chemistry, Texas A&M UniVersity, P.O. Box 30012, College Station, Texas 77842-3012. http://pubs.acs.org/cgi-bin/article.cgi/bichaw/2004/43/i18/pdf/bi049945+.pdf〕
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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