Enzyme

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     6. Ligases
        6.3 Forming carbon-nitrogen bonds
            6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor
ID:6.3.5.5
Description:Carbamoyl-phosphate synthase (glutamine-hydrolyzing).
Alternative Name: Glutamine-dependent carbamyl phosphate synthetase.
Glutamine-dependent carbamoyl-phosphate synthase.
GD-CPSase.
CPS.
Carbamyl phosphate synthetase (glutamine).
Carbamoylphosphate synthetase II.
Carbamoyl-phosphate synthetase (glutamine-hydrolyzing).
Carbamoyl phosphate synthetase.
Prosite: PDOC50975; PDOC00676; PDOC00405;
PDB:
PDBScop
Cath: 1.10.1030.10; 3.20.20.140; 3.30.1490.20; 3.30.470.20; 3.40.50.880; 3.50.30.20; 3.40.50.1370; 3.40.50.1380; 3.40.50.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.3.5.5
BRENDA Enzyme Link: BRENDA 6.3.5.5
KEGG Enzyme Link: KEGG6.3.5.5
BioCyc Enzyme Link: BioCyc 6.3.5.5
ExPASy Enzyme Link: ExPASy6.3.5.5
EC2PDB Enzyme Link: EC2PDB 6.3.5.5
ExplorEnz Enzyme Link: ExplorEnz 6.3.5.5
PRIAM enzyme-specific profiles Link: PRIAM 6.3.5.5
IntEnz Enzyme Link: IntEnz 6.3.5.5
MEDLINE Enzyme Link: MEDLINE 6.3.5.5
MSA:

6.3.5.5;

Phylogenetic Tree:

6.3.5.5;

Uniprot:
M-CSA:
RHEA:18633 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[*:5]=[C;H0;+0:6](-[OH;+0:7])-[OH;+0:8].[*:9]=[P;H0;+0:10](-[*:11])(-[*:12])-[O;H0;+0:13]-[*:14].[*:15]=[P;H0;+0:16](-[*:17])(-[*:18])-[O;H0;+0:19]-[*:20].[OH2;+0:21]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:7].[*:14]-[OH;+0:13].[*:20]-[OH;+0:19].[*:15]=[P;H0;+0:16](-[*:17])(-[*:18])-[O;H0;+0:8]-[C;H0;+0:6](=[*:5])-[NH2;+0:4].[*:9]=[P;H0;+0:10](-[*:11])(-[*:12])-[OH;+0:21]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Carbamoyl phosphate synthetase: a tunnel runs through it.Holden HM, Thoden JB, Raushel FM1998 Dec9914247
Carbamoyl phosphate synthetase: a crooked path from substrates to products.Raushel FM, Thoden JB, Reinhart GD, Holden HM1998 Oct9818189
Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase.Stapleton MA, Javid-Majd F, Harmon MF, Hanks BA, Grahmann JL, Mullins LS, Raushel FM1996 Nov 128916922
Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues.Yip MC, Knox WE1970 May 105442268
Purification and properties of a bacterial carbamyl phosphate synthetase.Kalman SM, Duffield PH, Brzozowski T1966 Apr 255329589
Evidence for an activated form of carbon dioxide in the reaction catalyzed by Escherichia coli carbamyl phosphate synthetase.Anderson PM, Meister A1965 Dec5326356
Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia.Thoden JB, Huang X, Raushel FM, Holden HM2002 Oct 1812130656
The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia.Raushel FM, Thoden JB, Holden HM1999 Jun 2210387030