Carbamoyl phosphate synthetase
From Proteopedia
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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. | 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. | ||
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==3D structures of carbamoyl phosphate synthetase== | ==3D structures of carbamoyl phosphate synthetase== |
Revision as of 13:12, 15 January 2019
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3D structures of carbamoyl phosphate synthetase
Updated on 15-January-2019
1jdb - EcCPS + phosphate + glutamine + ADP – Escherichia coli
1a9x, 1cs0 - EcCPS + phosphate + ornithine + ADP
1c30, 1m6v - EcCPS (mutant) + phosphate + ornithine + ADP
1bxr - EcCPS + ornithine + AMPPNP
1ce8 - EcCPS + phosphate + ornithine + inosinic acid + ADP
1c3o - EcCPS (mutant) + phosphate + ornithine + glutamine + ADP
1kee - EcCPS + phosphate + ornithine + acivicin + ADP
1t36 - EcCPS (mutant) + phosphate + ornithine + UMP + ADP
5dot – hCPS I – human
2yvq – CPS I MGS domain
5dou – hCPS I + phosphate + ADP
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