EC |
2.7.6.1 |
Accepted name: |
ribose-phosphate diphosphokinase |
Reaction: |
ATP + D-ribose 5-phosphate = AMP + 5-phospho-α-D-ribose 1-diphosphate |
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For diagram of ribose activation, click here |
Glossary: |
PRPP = 5-phospho-α-D-ribose 1-diphosphate |
Other name(s): |
ribose-phosphate pyrophosphokinase; PRPP synthetase; phosphoribosylpyrophosphate synthetase; PPRibP synthetase; PP-ribose P synthetase; 5-phosphoribosyl-1-pyrophosphate synthetase; 5-phosphoribose pyrophosphorylase; 5-phosphoribosyl-α-1-pyrophosphate synthetase; phosphoribosyl-diphosphate synthetase; phosphoribosylpyrophosphate synthase; pyrophosphoribosylphosphate synthetase; ribophosphate pyrophosphokinase; ribose-5-phosphate pyrophosphokinase |
Systematic name: |
ATP:D-ribose-5-phosphate diphosphotransferase |
Comments: |
dATP can also act as donor. |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9015-83-2 |
References: |
1. |
Hughes, D.E. and Williamson, D.H. Some properties of glutaminase of Clostridium welchii. Biochem. J. 51 (1952) 45–55. [PMID: 14944530] |
2. |
Hurlbert, R.B. and Reichard, P. The conversion of orotic acid to uridine nucleotides in vitro. Acta Chem. Scand. 9 (1955) 251–262. |
3. |
Remy, C.N., Remy, W.T. and Buchanan, J.M. Biosynthesis of the purines. VIII. Enzymatic synthesis and utilization of α-5-phosphoribosylpyrophosphate. J. Biol. Chem. 217 (1955) 885–895. [PMID: 13271449] |
4. |
Switzer, R.L. Regulation and mechanism of phosphoribosylpyrophosphate synthetase. I. Purification and properties of the enzyme from Salmonella typhimurium. J. Biol. Chem. 244 (1969) 2854–2863. [PMID: 4306285] |
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[EC 2.7.6.1 created 1961] |
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