Biology:5-(carboxyamino)imidazole ribonucleotide mutase
From HandWiki
Short description: Class of enzymes
| 5-(carboxyamino)imidazole ribonucleotide mutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.4.99.18 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a 5-(carboxyamino)imidazole ribonucleotide mutase (EC 5.4.99.18) is an enzyme that catalyzes the chemical reaction
- 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole [math]\displaystyle{ \rightleftharpoons }[/math] 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Hence, this enzyme has one substrate, 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole, and one product, 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole carboxymutase. Other names in common use include N5-CAIR mutase, PurE, N5-carboxyaminoimidazole ribonucleotide mutase, and class I PurE.
References
- "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. 1992. doi:10.1021/bi00136a016. PMID 1534690.
- "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. 1994. doi:10.1021/bi00174a038. PMID 8117684.
- "Evidence for the direct transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase". Biochemistry 38 (10): 3012–8. 1999. doi:10.1021/bi9827159. PMID 10074353.
- "Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway". Structure 7 (11): 1395–406. 1999. doi:10.1016/S0969-2126(00)80029-5. PMID 10574791.
- "Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms". Biochemistry 33 (39): 11927–34. 1994. doi:10.1021/bi00205a031. PMID 7918411.
- Davisson VJ; Misialek, S; Toffaletti, DL; Klem, TJ; Perfect, JR; Davisson, VJ (1998). "Biochemical role of the Cryptococcus neoformans ADE2 protein in fungal de novo purine biosynthesis". Arch. Biochem. Biophys. 351 (1): 123–34. doi:10.1006/abbi.1997.0512. PMID 9500840.
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