D
IPR010672

IMP biosynthesis enzyme PurP, N-terminal

InterPro entry
Short nameIMP_biosynth_PurP_N
Overlapping
homologous
superfamilies
 

Description

The last two steps ofde novopurine biosynthesis are:

     * 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)

In bacteria and eukaryotes, these steps are catalysed by the well-characterised bifunctional enzyme PurH
[1]
. Archaea do not appear to posses PurH, however, and perform these reactions by a different mecahnism
[2]
. In archaea, step i) is catalysed by the well-conserved PurP protein, while step ii) is catalysed by the PurO enzyme in some (though not all) species
[3, 4]
.

This entry represents the N-terminal domain of PurP. Its function is not known, though it is almost always found in association with
IPR009720
.

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

Cross References

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