Carbamoyl phosphate synthetase
From Proteopedia
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| - | <StructureSection load='1a9x' size=' | + | <StructureSection load='1a9x' size='350' side='right' scene='49/493669/Cv/4' caption='E. coli carbamoyl phosphate synthetase large chain (cyan) and small chain (salmon) complex with ADP, phosphate and ornithine, [[1a9x]]'> |
== Function == | == Function == | ||
| - | '''Carbamoyl phosphate synthetase''' (CPS) catalyzes the production of carbamoyl phosphate from ATP, Mg+2, bicarbonate | + | '''Carbamoyl 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.<ref>PMID:5329589</ref> There are 3 forms of CPS:<br /> |
* '''CPS I''' participates in the urea cycle. CPS I uses glutamine for NH3 source.<br /> | * '''CPS I''' participates in the urea cycle. CPS I uses glutamine for NH3 source.<br /> | ||
* '''CPS II''' participates in pyrimidine metabolism<br /> | * '''CPS II''' participates in pyrimidine metabolism<br /> | ||
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== Structural highlights == | == Structural highlights == | ||
| - | CPS 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. CPS I contains a methylglyoxal synthetase (MGS) domain which binds ornithine. | + | CPS 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 <scene name='49/493669/Cv/3'>small subunit active site contains an active Cys residue</scene>.<ref>PMID:9636022</ref> CPS I contains a methylglyoxal synthetase (MGS) domain which binds <scene name='49/493669/Cv/6'>L-ornithine</scene>. Water molecules are shown as red spheres. |
| - | </ | + | |
| + | <scene name='49/493669/Cv/11'>ADP binding site</scene>. | ||
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| + | <scene name='49/493669/Cv/12'>Mn coordination site</scene>. | ||
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| + | <scene name='49/493669/Cv/13'>K coordination site</scene>. | ||
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==3D structures of carbamoyl phosphate synthetase== | ==3D structures of carbamoyl phosphate synthetase== | ||
| + | [[Carbamoyl phosphate synthetase 3D structures]] | ||
| - | + | </StructureSection> | |
| - | + | == References == | |
| - | + | <references/> | |
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Kalman SM, Duffield PH, Brzozowski T. Purification and properties of a bacterial carbamyl phosphate synthetase. J Biol Chem. 1966 Apr 25;241(8):1871-7. PMID:5329589
- ↑ Thoden JB, Miran SG, Phillips JC, Howard AJ, Raushel FM, Holden HM. Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis. Biochemistry. 1998 Jun 23;37(25):8825-31. PMID:9636022 doi:http://dx.doi.org/10.1021/bi9807761
