EC |
2.4.2.7 |
Accepted name: |
adenine phosphoribosyltransferase |
Reaction: |
AMP + diphosphate = adenine + 5-phospho-α-D-ribose 1-diphosphate |
|
For diagram of ribose activation, click here |
Other name(s): |
AMP pyrophosphorylase; transphosphoribosidase; APRT; AMP-pyrophosphate phosphoribosyltransferase; adenine phosphoribosylpyrophosphate transferase; adenosine phosphoribosyltransferase; adenylate pyrophosphorylase; adenylic pyrophosphorylase |
Systematic name: |
AMP:diphosphate phospho-D-ribosyltransferase |
Comments: |
5-Amino-4-imidazolecarboxamide can replace adenine. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-80-9 |
References: |
1. |
Flaks, J.G., Erwin, M.J. and Buchanan, J.M. Biosynthesis of the purines. XVI. The synthesis of adenosine 5′-phosphate and 5-amino-4-imidazolecarboxamide ribotide by a nucleotide pyrophosphorylase. J. Biol. Chem. 228 (1957) 201–213. [PMID: 13475309] |
2. |
Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417–427. [PMID: 14392175] |
3. |
Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432–433. [PMID: 13436452] |
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[EC 2.4.2.7 created 1961] |
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EC |
2.4.2.8 |
Accepted name: |
hypoxanthine phosphoribosyltransferase |
Reaction: |
IMP + diphosphate = hypoxanthine + 5-phospho-α-D-ribose 1-diphosphate |
Other name(s): |
IMP pyrophosphorylase; transphosphoribosidase; hypoxanthine—guanine phosphoribosyltransferase; guanine phosphoribosyltransferase; GPRT; HPRT; guanosine 5′-phosphate pyrophosphorylase; IMP-GMP pyrophosphorylase; HGPRTase; 6-hydroxypurine phosphoribosyltransferase; 6-mercaptopurine phosphoribosyltransferase; GMP pyrophosphorylase; guanine-hypoxanthine phosphoribosyltransferase; guanosine phosphoribosyltransferase; guanylate pyrophosphorylase; guanylic pyrophosphorylase; inosinate pyrophosphorylase; inosine 5′-phosphate pyrophosphorylase; inosinic acid pyrophosphorylase; inosinic pyrophosphorylase; purine-6-thiol phosphoribosyltransferase |
Systematic name: |
IMP:diphosphate phospho-D-ribosyltransferase |
Comments: |
Guanine and purine-6-thiol can replace hypoxanthine. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9016-12-0 |
References: |
1. |
Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136–158. |
2. |
Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417–427. [PMID: 14392175] |
3. |
Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432–433. [PMID: 13436452] |
4. |
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] |
|
[EC 2.4.2.8 created 1961, modified 1982] |
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EC |
2.4.2.9 |
Accepted name: |
uracil phosphoribosyltransferase |
Reaction: |
UMP + diphosphate = uracil + 5-phospho-α-D-ribose 1-diphosphate |
Other name(s): |
UMP pyrophosphorylase; UPRTase; UMP:pyrophosphate phosphoribosyltransferase; uridine 5′-phosphate pyrophosphorylase; uridine monophosphate pyrophosphorylase; uridylate pyrophosphorylase; uridylic pyrophosphorylase |
Systematic name: |
UMP:diphosphate phospho-α-D-ribosyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-24-4 |
References: |
1. |
Crawford, I., Kornberg, A. and Simms, E.S. Conversion of uracil and orotate to uridine 5′-phosphate by enzymes in lactobacilli. J. Biol. Chem. 226 (1967) 1093–1101. [PMID: 13438895] |
2. |
Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136–158. |
|
[EC 2.4.2.9 created 1961] |
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EC |
2.4.2.10 |
Accepted name: |
orotate phosphoribosyltransferase |
Reaction: |
orotidine 5′-phosphate + diphosphate = orotate + 5-phospho-α-D-ribose 1-diphosphate |
|
For diagram of pyrimidine biosynthesis, click here |
Other name(s): |
orotidylic acid phosphorylase; orotidine-5′-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5′-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase |
Systematic name: |
orotidine-5′-phosphate:diphosphate phospho-α-D-ribosyl-transferase |
Comments: |
The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5′-phosphate decarboxylase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-25-5 |
References: |
1. |
Jones, M.E., Kavipurapu, P.R. and Traut, T.W. Orotate phosphoribosyltransferase: orotidylate decarboxylase (Ehrlich ascites cell). Methods Enzymol. 51 (1978) 155–167. [DOI] [PMID: 692383] |
2. |
Lieberman, I., Kornberg, A. and Simms, E.S. Enzymatic synthesis of pyrimidine nucleotides. Orotidine-5′-phosphate and uridine-5′-phosphate. J. Biol. Chem. 215 (1955) 403–415. [PMID: 14392174] |
3. |
McClard, R.W., Black, M.J., Livingstone, L.R. and Jones, M.E. Isolation and initial characterization of the single polypeptide that synthesizes uridine 5′-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5′-monophosphate synthase. Biochemistry 19 (1980) 4699–4706. [PMID: 6893554] |
|
[EC 2.4.2.10 created 1961, modified 1986] |
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EC
|
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 |
2.4.2.12 |
Accepted name: |
nicotinamide phosphoribosyltransferase |
Reaction: |
nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-α-D-ribose 1-diphosphate |
|
For diagram of NADP+ biosynthesis, click here |
Other name(s): |
NMN pyrophosphorylase; nicotinamide mononucleotide pyrophosphorylase; nicotinamide mononucleotide synthetase; NMN synthetase; nicotinamide-nucleotide:diphosphate phospho-α-D-ribosyltransferase |
Systematic name: |
nicotinamide-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-27-7 |
References: |
1. |
Preiss, J. and Handler, P. Enzymatic synthesis of nicotinamide mononucleotide. J. Biol. Chem. 225 (1957) 759–770. [PMID: 13416279] |
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[EC 2.4.2.12 created 1961] |
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EC |
2.4.2.14 |
Accepted name: |
amidophosphoribosyltransferase |
Reaction: |
5-phospho-β-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-α-D-ribose 1-diphosphate + H2O |
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For diagram of ribose activation, click here |
Other name(s): |
phosphoribosyldiphosphate 5-amidotransferase; glutamine phosphoribosyldiphosphate amidotransferase; α-5-phosphoribosyl-1-pyrophosphate amidotransferase; 5′-phosphoribosylpyrophosphate amidotransferase; 5-phosphoribosyl-1-pyrophosphate amidotransferase; 5-phosphororibosyl-1-pyrophosphate amidotransferase; glutamine 5-phosphoribosylpyrophosphate amidotransferase; glutamine ribosylpyrophosphate 5-phosphate amidotransferase; phosphoribose pyrophosphate amidotransferase; phosphoribosyl pyrophosphate amidotransferase; phosphoribosylpyrophosphate glutamyl amidotransferase; 5-phosphoribosylamine:diphosphate phospho-α-D-ribosyltransferase (glutamate-amidating) |
Systematic name: |
5-phospho-β-D-ribosylamine:diphosphate phospho-α-D-ribosyltransferase (glutamate-amidating) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-82-7 |
References: |
1. |
Caskey, C.T., Ashton, D.M. and Wyngaarden, J.B. The enzymology of feedback inhibition of glutamine phosphoribosylpyrophosphate amidotransferase by purine ribonucleotides. J. Biol. Chem. 239 (1964) 2570–2579. [PMID: 14235537] |
2. |
Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXI. 5-Phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 233 (1958) 451–455. [PMID: 13563519] |
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[EC 2.4.2.14 created 1961] |
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EC |
2.4.2.17 |
Accepted name: |
ATP phosphoribosyltransferase |
Reaction: |
1-(5-phospho-β-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-α-D-ribose 1-diphosphate |
|
For diagram of histidine biosynthesis (early stages), click here |
Other name(s): |
phosphoribosyl-ATP pyrophosphorylase; adenosine triphosphate phosphoribosyltransferase; phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase; phosphoribosyl ATP synthetase; phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase; phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase; phosphoribosyladenosine triphosphate pyrophosphorylase; phosphoribosyladenosine triphosphate synthetase; 1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase |
Systematic name: |
1-(5-phospho-β-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase |
Comments: |
Involved in histidine biosynthesis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-46-3 |
References: |
1. |
Ames, B.N., Martin, R.G. and Garry, B.J. The first step of histidine biosynthesis. J. Biol. Chem. 236 (1961) 2019–2026. [PMID: 13682989] |
2. |
Martin, R.G. The phosphorolysis of nucleosides by rabbit bone marrow: The nature of feedback inhibition by histidine. J. Biol. Chem. 238 (1963) 257–268. |
3. |
Voll, M.J., Appella, E. and Martin, R.G. Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis. J. Biol. Chem. 242 (1967) 1760–1767. [PMID: 5337591] |
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[EC 2.4.2.17 created 1972] |
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EC |
2.4.2.18 |
Accepted name: |
anthranilate phosphoribosyltransferase |
Reaction: |
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-α-D-ribose 1-diphosphate |
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For diagram of tryptophan biosynthesis, click here |
Other name(s): |
phosphoribosyl-anthranilate pyrophosphorylase; PRT; anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase; anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase; phosphoribosylanthranilate pyrophosphorylase; phosphoribosylanthranilate transferase; anthranilate-PP-ribose-P phosphoribosyltransferase |
Systematic name: |
N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-α-D-ribosyltransferase |
Comments: |
In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-35-2 |
References: |
1. |
Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365–380. |
2. |
Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [DOI] [PMID: 3535653] |
3. |
Ito, J. and Yanofsky, C. Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits. J. Bacteriol. 97 (1969) 734–742. [PMID: 4886290] |
4. |
Wegman, J. and DeMoss, J.A. The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa. J. Biol. Chem. 240 (1965) 3781–3788. [PMID: 5842052] |
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[EC 2.4.2.18 created 1972] |
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EC |
2.4.2.19 |
Accepted name: |
nicotinate-nucleotide diphosphorylase (carboxylating) |
Reaction: |
β-nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-α-D-ribose 1-diphosphate |
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For diagram of NAD+ biosynthesis, click here |
Glossary: |
quinolinate = pyridine-2,3-dicarboxylate |
Other name(s): |
quinolinate phosphoribosyltransferase (decarboxylating); quinolinic acid phosphoribosyltransferase; QAPRTase; NAD+ pyrophosphorylase; nicotinate mononucleotide pyrophosphorylase (carboxylating); quinolinic phosphoribosyltransferase |
Systematic name: |
β-nicotinate-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating) |
Comments: |
The reaction is catalysed in the opposite direction. Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD+ biosynthesis enzyme shared by both eukaryotes and prokaryotes [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-74-0 |
References: |
1. |
Gholson, R.K., Ueda, I., Ogasawara, N. and Henderson, L.M. The enzymatic conversion of quinolinate to nicotinic acid mononucleotide in mammalian liver. J. Biol. Chem. 239 (1964) 1208–1214. [PMID: 14165928] |
2. |
Packman, P.M. and Jakoby, W.B. Crystalline quinolinate phosphoribosyltransferase. J. Biol. Chem. 240 (1965) 4107–4108. [PMID: 5320648] |
3. |
Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid. Plant Physiol. 141 (2006) 851–857. [DOI] [PMID: 16698895] |
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[EC 2.4.2.19 created 1972] |
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EC |
2.4.2.20 |
Accepted name: |
dioxotetrahydropyrimidine phosphoribosyltransferase |
Reaction: |
a 2,4-dioxotetrahydropyrimidine D-ribonucleotide + diphosphate = a 2,4-dioxotetrahydropyrimidine + 5-phospho-α-D-ribose 1-diphosphate |
Other name(s): |
dioxotetrahydropyrimidine-ribonucleotide pyrophosphorylase; dioxotetrahydropyrimidine phosphoribosyl transferase; dioxotetrahydropyrimidine ribonucleotide pyrophosphorylase; 2,4-dioxotetrahydropyrimidine-nucleotide:diphosphate phospho-α-D-ribosyltransferase |
Systematic name: |
2,4-dioxotetrahydropyrimidine-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase |
Comments: |
Acts (in the reverse direction) on uracil and other pyrimidines and pteridines containing a 2,4-diketo structure. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-75-1 |
References: |
1. |
Hatfield, D. and Wyngaarden, J.B. 3-Ribosylpurines. I. Synthesis of (3-ribosyluric acid) 5′-phosphate and (3-ribosylxanthine) 5′-phosphate by a pyrimidine ribonucleotide pyrophosphorylase of beef erythrocytes. J. Biol. Chem. 239 (1964) 2580–2586. [PMID: 14235538] |
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[EC 2.4.2.20 created 1972] |
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EC |
2.4.2.22 |
Accepted name: |
xanthine phosphoribosyltransferase |
Reaction: |
XMP + diphosphate = 5-phospho-α-D-ribose 1-diphosphate + xanthine |
Glossary: |
XMP = 9-(5-phospho-β-D-ribosyl)xanthine = xanthosine 5′-phosphate |
Other name(s): |
Xan phosphoribosyltransferase; xanthosine 5′-phosphate pyrophosphorylase; xanthylate pyrophosphorylase; xanthylic pyrophosphorylase; XMP pyrophosphorylase; 5-phospho-α-D-ribose-1-diphosphate:xanthine phospho-D-ribosyltransferase; 9-(5-phospho-β-D-ribosyl)xanthine:diphosphate 5-phospho-α-D-ribosyltransferase |
Systematic name: |
XMP:diphosphate 5-phospho-α-D-ribosyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-10-3 |
References: |
1. |
Krenitsky, T.A., Neil, S.M. and Miller, R.L. Guanine and xanthine phosphoribosyltransfer activities of Lactobacillus casei and Escherichia coli. Their relationship to hypoxanthine and adenine phosphoribosyltransfer activities. J. Biol. Chem. 245 (1970) 2605–2611. [PMID: 4910918] |
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[EC 2.4.2.22 created 1972] |
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EC |
2.4.2.45 |
Accepted name: |
decaprenyl-phosphate phosphoribosyltransferase |
Reaction: |
trans,octacis-decaprenyl phosphate + 5-phospho-α-D-ribose 1-diphosphate = trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate + diphosphate |
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For diagram of decaprenylphosphoarabinofuranose biosynthesis, click here |
Other name(s): |
5-phospho-α-D-ribose-1-diphosphate:decaprenyl-phosphate 5-phosphoribosyltransferase; 5-phospho-α-D-ribose 1-pyrophosphate:decaprenyl phosphate 5-phosphoribosyltransferase; DPPR synthase; Rv3806 |
Systematic name: |
trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate:diphosphate phospho-α-D-ribosyltransferase |
Comments: |
Requires Mg2+. Isolated from Mycobacterium tuberculosis. Has some activity with other polyprenyl phosphates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Huang, H., Scherman, M.S., D'Haeze, W., Vereecke, D., Holsters, M., Crick, D.C. and McNeil, M.R. Identification and active expression of the Mycobacterium tuberculosis gene encoding 5-phospho-α-D-ribose-1-diphosphate: decaprenyl-phosphate 5-phosphoribosyltransferase, the first enzyme committed to decaprenylphosphoryl-D-arabinose synthesis. J. Biol. Chem. 280 (2005) 24539–24543. [DOI] [PMID: 15878857] |
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[EC 2.4.2.45 created 2012] |
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EC |
2.4.2.49 |
Accepted name: |
neamine phosphoribosyltransferase |
Reaction: |
neamine + 5-phospho-α-D-ribose 1-diphosphate = 5′′-phosphoribostamycin + diphosphate |
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For diagram of neamine and ribostamycin biosynthesis, click here |
Glossary: |
neamine = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl]oxy}oxane-3,4-diol
ribostamycin = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2-{[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-3-hydroxycyclohexyl]oxy}oxane-3,4-diol |
Other name(s): |
btrL (gene name); neoM (gene name) |
Systematic name: |
neamine:5-phospho-α-D-ribose 1-diphosphate phosphoribosyltransferase |
Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin. The enzyme requires a divalent metal ion, optimally Mg2+, Ni2+ or Co2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kudo, F., Fujii, T., Kinoshita, S. and Eguchi, T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg. Med. Chem. 15 (2007) 4360–4368. [DOI] [PMID: 17482823] |
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[EC 2.4.2.49 created 2013] |
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EC |
2.4.2.54 |
Accepted name: |
β-ribofuranosylphenol 5′-phosphate synthase |
Reaction: |
5-phospho-α-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(β-D-ribofuranosyl)phenol 5′-phosphate + CO2 + diphosphate |
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For diagram of methanopterin biosynthesis (part 2), click here |
Other name(s): |
β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); β-ribofuranosylhydroxybenzene 5′-phosphate synthase; 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5′-phosphate synthase (incorrect); 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) (incorrect) |
Systematic name: |
5-phospho-α-D-ribose-1-diphosphate:4-hydroxybenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) |
Comments: |
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It can utilize both 4-hydroxybenzoate and 4-aminobenzoate as substrates, but only the former is known to be produced by methanogenic archaea [4]. The activity is dependent on Mg2+ or Mn2+ [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rasche, M.E. and White, R.H. Mechanism for the enzymatic formation of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate during the biosynthesis of methanopterin. Biochemistry 37 (1998) 11343–11351. [DOI] [PMID: 9698382] |
2. |
Scott, J.W. and Rasche, M.E. Purification, overproduction, and partial characterization of β-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway. J. Bacteriol. 184 (2002) 4442–4448. [DOI] [PMID: 12142414] |
3. |
Dumitru, R.V. and Ragsdale, S.W. Mechanism of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway. J. Biol. Chem. 279 (2004) 39389–39395. [DOI] [PMID: 15262968] |
4. |
White, R.H. The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin. Biochemistry 50 (2011) 6041–6052. [DOI] [PMID: 21634403] |
5. |
Bechard, M.E., Farahani, P., Greene, D., Pham, A., Orry, A. and Rasche, M.E. Purification, kinetic characterization, and site-directed mutagenesis of Methanothermobacter thermautotrophicus RFAP synthase produced in Escherichia coli. AIMS Microbiol 5 (2019) 186–204. [DOI] [PMID: 31663056] |
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[EC 2.4.2.54 created 2013, modified 2014, modified 2015] |
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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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