Carbamoyl phosphate synthetase
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ContentsFunctionCarbamoyl phosphate synthetase (CPS) catalyzes the production of carbamoyl phosphate from ATP, Mg+2, bicarbonate and glutamine. CPS is part of the pyrimidine and arginine biosynthesis as well as the urea cycle in vertebrates. Ornithine is an allosteric effector of CPS.[1] There are 3 forms of CPS:
DiseaseCPS I deficiency causes the accumulation of NH3 in the blood. Structural highlightsCPS I and II are composed of 2 subunits. The large subunit contain active sites which bind nucleotides and other effectors. The small subunit catalyzes the hydrolysis of glutamine to glutamate and NH3. The small subunit active site contains an active Cys residue.[2] CPS I contains a methylglyoxal synthetase (MGS) domain which binds L-ornithine. Water molecules are shown as red spheres. 3D structures of carbamoyl phosphate synthetaseCarbamoyl phosphate synthetase 3D structures
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This page was last modified 09:15, 22 April 2019.