| EC |
2.7.4.23 |
| Accepted name: |
ribose 1,5-bisphosphate phosphokinase |
| Reaction: |
ATP + α-D-ribose 1,5-bisphosphate = ADP + 5-phospho-α-D-ribose 1-diphosphate |
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For diagram of AMP catabolism, click here |
| Glossary: |
5-phospho-α-D-ribose 1-diphosphate = PRPP |
| Other name(s): |
ribose 1,5-bisphosphokinase; PhnN; ATP:ribose-1,5-bisphosphate phosphotransferase |
| Systematic name: |
ATP:α-D-ribose-1,5-bisphosphate phosphotransferase |
| Comments: |
This enzyme, found in NAD supression mutants of Escherichia coli, synthesizes 5-phospho-α-D-ribose 1-diphosphate (PRPP) without the participation of EC 2.7.6.1, ribose-phosphate diphosphokinase. Ribose, ribose 1-phosphate and ribose 5-phosphate are not substrates, and GTP cannot act as a phosphate donor. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Hove-Jensen, B., Rosenkrantz, T.J., Haldimann, A. and Wanner, B.L. Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways. J. Bacteriol. 185 (2003) 2793–2801. [DOI] [PMID: 12700258] |
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| [EC 2.7.4.23 created 2006] |
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