220.127.116.11 - Amidophosphoribosyltransferase
- Phosphoribosyldiphosphate 5-amidotransferase.
- Glutamine phosphoribosylpyrophosphate amidotransferase.
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
There are no Cofactors for this Enzyme
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
intermediate formation, intermediate terminated, native state of enzyme regenerated, overall reactant used, dephosphorylation, bimolecular nucleophilic addition, unimolecular elimination by the conjugate base, proton relay, bimolecular nucleophilic substitution, enzyme-substrate complex formation, enzyme-substrate complex cleavage, deamination, intermediate collapse, proton transfer, overall product formed
Reaction occurs in the PRTase Domain. The conformation of the enzyme-bound Mn-cPRPP for catalysis as it favours the formation of a tri- or pentavalent intermediate with some double bond character in the ribose C1-O4 bond. . The step is described as an in-line displacement in which ammonia attacks the C1 of the 5-Phospho-alpha-D-ribose-1-diphosphate substrate in a nucleophilic substitution. The product pyrophosphate deprotonates the newly attached ammonia. However, it is unclear whether the intermediate is actually a transition state. There are no residues that are essential for catalytic activity, however the Tyr258 is probably stabilising [PMID:9914248].
- Kinetic Parameters
There are no reaction parameters information for this Enzyme.
Organism pH Range Comment Glycine max 6 - 10 approx. 70% of maximal activity between pH 6 and pH 10 Schizosaccharomyces pombe 7 - 9 stable enzyme, approx. 65% and unstable enzyme approx. 70% of maximal activity at pH 7, stable enzyme, approx. 75% and unstable enzyme approx. 65% of maximal activity at pH 9
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