PROSITE documentation PDOC00105Phosphoribosyl pyrophosphate synthase signature
Phosphoribosyl pyrophosphate synthase (EC 2.7.6.1) (PRPP synthase) catalyzes the formation of PRPP from ATP and ribose 5-phosphate. PRPP is then used in various biosynthetic pathways, as for example in the formation of purines, pyrimidines, histidine and tryptophan. PRPP synthase requires inorganic phosphate and magnesium ions for its stability and activity.
In mammals, three isozymes of PRPP synthase are found; in yeast there are at least four isozymes.
As a signature pattern for this enzyme, we selected a very conserved region that has been suggested to be involved in binding divalent cations [1]. This region contains two conserved aspartic acid residues as well as a histidine, which are all potential ligands for a cation such as magnesium.
Last update:April 2006 / Pattern revised.
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| 1 | Authors | Bower S.G. Harlow K.W. Switzer R.L. Hove-Jensen B. |
| Title | Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site. | |
| Source | J. Biol. Chem. 264:10287-10291(1989). | |
| PubMed ID | 2542328 |
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