IMP biosynthesis enzyme PurP, N-terminal
Short name | IMP_biosynth_PurP_N |
Overlapping homologous superfamilies |
Description
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* conversion of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate (FAICAR)
* conversion of FAICAR to inosine5'-monophopsphate (IMP)
References
1.Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis. Greasley SE, Horton P, Ramcharan J, Beardsley GP, Benkovic SJ, Wilson IA. Nat. Struct. Biol. 8, 402-6, (2001). View articlePMID: 11323713
2.Purine biosynthesis in the domain Archaea without folates or modified folates. White RH. J. Bacteriol. 179, 3374-7, (1997). View articlePMID: 9150241
3.A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase. A new enzyme in purine biosynthesis. Ownby K, Xu H, White RH. J. Biol. Chem. 280, 10881-7, (2005). View articlePMID: 15623504
4.New class of IMP cyclohydrolases in Methanococcus jannaschii. Graupner M, Xu H, White RH. J. Bacteriol. 184, 1471-3, (2002). View articlePMID: 11844782
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- Pfam:PF06849