EC
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2.4.2.11
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Transferred entry: | nicotinate phosphoribosyltransferase. Now EC 6.3.4.21, nicotinate phosphoribosyltransferase.
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[EC 2.4.2.11 created 1961, deleted 2013] |
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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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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, 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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EC |
6.3.4.21 |
Accepted name: |
nicotinate phosphoribosyltransferase |
Reaction: |
nicotinate + 5-phospho-α-D-ribose 1-diphosphate + ATP + H2O = β-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate |
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For diagram of NAD+ biosynthesis, click here |
Other name(s): |
niacin ribonucleotidase; nicotinic acid mononucleotide glycohydrolase; nicotinic acid mononucleotide pyrophosphorylase; nicotinic acid phosphoribosyltransferase; nicotinate-nucleotide:diphosphate phospho-α-D-ribosyltransferase |
Systematic name: |
5-phospho-α-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming) |
Comments: |
The enzyme, which is involved in pyridine nucleotide recycling, can form β-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-α-D-ribose 1-diphosphate (PRPP) in the absence of ATP. However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate. The phospho-enzyme is hydrolysed during the transferase reaction, regenerating the low affinity form. The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100 [4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-26-6 |
References: |
1. |
Imsande, J. Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli. J. Biol. Chem. 236 (1961) 1494–1497. [PMID: 13717628] |
2. |
Imsande, J. and Handler, P. Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid mononucleotide pyrophosphorylase. J. Biol. Chem. 236 (1961) 525–530. [PMID: 13717627] |
3. |
Kosaka, A., Spivey, H.O. and Gholson, R.K. Nicotinate phosphoribosyltransferase of yeast. Purification and properties. J. Biol. Chem. 246 (1971) 3277–3283. [PMID: 4324895] |
4. |
Vinitsky, A. and Grubmeyer, C. A new paradigm for biochemical energy coupling. Salmonella typhimurium nicotinate phosphoribosyltransferase. J. Biol. Chem. 268 (1993) 26004–26010. [PMID: 7503993] |
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[EC 6.3.4.21 created 1961 as EC 2.4.2.11, transferred 2013 to EC 6.3.4.21] |
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