EC |
2.7.4.1 |
Accepted name: |
ATP-polyphosphate phosphotransferase |
Reaction: |
ATP + (phosphate)n = ADP + (phosphate)n+1 |
Other name(s): |
polyphosphate kinase 1; ppk1 (gene name); polyphosphate kinase (ambiguous); polyphosphoric acid kinase (ambiguous) |
Systematic name: |
ATP:polyphosphate phosphotransferase |
Comments: |
The enzyme is responsible for the synthesis of most of the cellular polyphosphate, using the terminal phosphate of ATP as substrate. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-44-2 |
References: |
1. |
Hoffmann-Ostenhof, O., Kenedy, J., Keck, K., Gabriel, O. and Schönfellinger, H.W. En neues Phosphat-übertragendes Ferment aus Hefe. Biochim. Biophys. Acta 14 (1954) 285. [PMID: 13172250] |
2. |
Kornberg, A., Kornberg, S.R. and Simms, E.S. Metaphosphate synthesis by an enzyme from Escherichia coli. Biochim. Biophys. Acta 20 (1956) 215–227. [DOI] [PMID: 13315368] |
3. |
Muhammed, A. Studies on biosynthesis of polymetaphosphate by an enzyme from Corynebacterium xerosis. Biochim. Biophys. Acta 54 (1961) 121–132. [DOI] [PMID: 14476999] |
4. |
Ahn, K. and Kornberg, A. Polyphosphate kinase from Escherichia coli. Purification and demonstration of a phosphoenzyme intermediate. J. Biol. Chem. 265 (1990) 11734–11739. [PMID: 2164013] |
5. |
Kumble, K.D., Ahn, K. and Kornberg, A. Phosphohistidyl active sites in polyphosphate kinase of Escherichia coli. Proc. Natl. Acad. Sci. USA 93 (1996) 14391–14395. [PMID: 8962061] |
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[EC 2.7.4.1 created 1961, modified 2021] |
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