5-(carboxyamino)imidazole ribonucleotide synthase
(Redirected from N5-carboxyaminoimidazole ribonucleotide synthetase)
| 5-(Carboxyamino)imidazole ribonucleotide synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.4.18 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a 5-(carboxyamino)imidazole ribonucleotide synthase (EC 6.3.4.18) is an enzyme that catalyzes the chemical reaction
- ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3− ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
The 3 substrates of this enzyme are ATP, 5-amino-1-(5-phospho-D-ribosyl)imidazole ("AIR"), and HCO3−, whereas its 3 products are ADP, phosphate, and 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is 5-amino-1-(5-phospho-D-ribosyl)imidazole:carbon-dioxide ligase (ADP-forming).
References
- Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM (1992). "Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway". Biochemistry. 31 (21): 5022–32. doi:10.1021/bi00136a016. PMID 1534690.
- Mueller EJ, Meyer E, Rudolph J, Davisson VJ, Stubbe J (1994). "N5-carboxyaminoimidazole ribonucleotide: evidence for a new intermediate and two new enzymatic activities in the de novo purine biosynthetic pathway of Escherichia coli". Biochemistry. 33 (8): 2269–78. doi:10.1021/bi00174a038. PMID 8117684.
- Thoden JB, Kappock TJ, Stubbe J, Holden HM (1999). "Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily". Biochemistry. 38 (47): 15480–92. doi:10.1021/bi991618s. PMID 10569930.
