Accepted name: uridine phosphorylase
Reaction: uridine + phosphate = uracil + α-D-ribose 1-phosphate
Other name(s): pyrimidine phosphorylase; UrdPase; UPH; UPase
Systematic name: uridine:phosphate α-D-ribosyltransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9030-22-2
References:
1. Canellakis, E.S. Pyrimidine metabolism. II. Enzymatic pathways of uracil anabolism. J. Biol. Chem. 227 (1957) 329-338.
2. Paege, L.M. and Schlenk, F. Bacterial uracil riboside phosphorylase. Arch. Biochem. Biophys. 40 (1952) 42-49.
3. Pontis, H., Degerstedt, G. and Reichard, P. Uridine and deoxyuridine phosphorylases from Ehrlich ascites tumor. Biochim. Biophys. Acta 51 (1961) 138-147.
Accepted name: thymidine phosphorylase
Reaction: thymidine + phosphate = thymine + 2-deoxy-α-D-ribose 1-phosphate
Other name(s): pyrimidine phosphorylase; thymidine-orthophosphate deoxyribosyltransferase; animal growth regulators, blood platelet-derived endothelial cell growth factors; blood platelet-derived endothelial cell growth factor; deoxythymidine phosphorylase; gliostatins; pyrimidine deoxynucleoside phosphorylase; thymidine:phosphate deoxy-D-ribosyltransferase
Systematic name: thymidine:phosphate deoxy-α-D-ribosyltransferase
Comments: The enzyme in some tissues also catalyses deoxyribosyltransferase reactions of the type catalysed by EC 2.4.2.6, nucleoside deoxyribosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9030-23-3
References:
1. Friedkin, M. and Roberts, D. The enzymatic synthesis of nucleosides. I. Thymidine phosphorylase in mammalian tissue. J. Biol. Chem. 207 (1954) 245-256.
2. Zimmerman, M. and Seidenberg, J. Deoxyribosyl transfer. I. Thymidine phosphorylase and nucleoside deoxyribosyltransferase in normal and malignant tissues. J. Biol. Chem. 239 (1964) 2618-2621.
3. Zimmerman, M. Deoxyribosyl transfer. II. Nucleoside:pyrimidine deoxyribosyltransferase activity of three partially purified thymidine phosphorylases. J. Biol. Chem. 239 (1964) 2622-2627.
Accepted name: nucleoside ribosyltransferase
Reaction: D-ribosyl-base1 + base2 = D-ribosyl-base2 + base1
Other name(s): nucleoside N-ribosyltransferase
Systematic name: nucleoside:purine(pyrimidine) D-ribosyltransferase
Comments: Base1 and base2 represent various purines and pyrimidines.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9030-31-3
References:
1. Koch, A.L. Some enzymes of nucleoside metabolism of Escherichia coli. J. Biol. Chem. 223 (1956) 535-549.
Accepted name: nucleoside deoxyribosyltransferase
Reaction: 2-deoxy-D-ribosyl-base1 + base2 = 2-deoxy-D-ribosyl-base2 + base1
Other name(s): purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl transferase; deoxyribose transferase; nucleoside trans-N-deoxyribosylase; trans-deoxyribosylase; trans-N-deoxyribosylase; trans-N-glycosidase; nucleoside deoxyribosyltransferase I (purine nucleoside:purine deoxyribosyltransferase: strictly specific for transfer between purine bases); nucleoside deoxyribosyltransferase II [purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyltransferase]
Systematic name: nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase
Comments: Base1 and base2 represent various purines and pyrimidines.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9026-86-2
References:
1. Kalckar, H.M., MacNutt, W.S. and Hoff-Jørgensen, E. Trans-N-glycosidase studied with radioactive adenine. Biochem. J. 50 (1952) 397-400.
2. MacNutt, W.S. The enzymically catalysed transfer of the deoxyribosyl group from one purine or pyrimidine to another. Biochem. J. 50 (1952) 384-397.
3. Roush, A.H. and Betz, R.F. Purification and properties of trans-N-deoxyribosylase. J. Biol. Chem. 233 (1958) 261-266.
Accepted name: adenine phosphoribosyltransferase
Reaction: AMP + diphosphate = adenine + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction 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, 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.
2. Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417-427.
3. Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432-433.
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; 6-mercaptopurine phosphoribosyltransferase; purine-6-thiol phosphoribosyltransferase
Systematic name: IMP:diphosphate phospho-D-ribosyltransferase
Comments: Guanine and 6-mercaptopurine can replace hypoxanthine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, 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.
3. Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432-433.
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.
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, 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.
2. Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136-158.
Accepted name: orotate phosphoribosyltransferase
Reaction: orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-α-D-ribose 1-diphosphate
For diagram 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, 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. [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.
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]
Accepted name: nicotinate phosphoribosyltransferase
Reaction: nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction 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: nicotinate-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, 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.
2. Imsande, J. and Handler, P. Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid mononucleotide pyrophosphorylase. J. Biol. Chem. 236 (1961) 525-530.
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]
Accepted name: nicotinamide phosphoribosyltransferase
Reaction: nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction 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, 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.
[EC 2.4.2.13 Transferred entry: now EC 2.5.1.6 methionine adenosyltransferase (EC 2.4.2.13 created 1961, deleted 1965)]
Accepted name: amidophosphoribosyltransferase
Reaction: 5-phospho-β-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-α-D-ribose 1-diphosphate + H2O
For diagram 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, 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.
2. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXI. 5-Phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 233 (1958) 451-455.
Accepted name: guanosine phosphorylase
Reaction: guanosine + phosphate = guanine + α-D-ribose 1-phosphate
Other Name(s): guanosine:phosphate D-ribosyltransferase
Systematic name: guanosine:phosphate α-D-ribosyltransferase
Comments: Also acts on deoxyguanosine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number: 9030-28-8
References:
1. Yamada, E.W. The phosphorolysis of nucleosides by rabbit bone marrow. J. Biol. Chem. 236 (1961) 3043-3046.
Accepted name: urate-ribonucleotide phosphorylase
Reaction: urate D-ribonucleotide + phosphate = urate + α-D-ribose 1-phosphate
Other name(s): UAR phosphorylase; urate-ribonucleotide:phosphate D-ribosyltransferase; urate-ribonucleotide:phosphate α-D-ribosyltransferase
Systematic name: urate-D-ribonucleotide:phosphate α-D-ribosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9030-29-9
References:
1. Laster, L. and Blair, A. An intestinal phosphorylase for uric acid ribonucleoside. J. Biol. Chem. 238 (1963) 3348-3357.
Accepted name: ATP phosphoribosyltransferase
Reaction: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-α-D-ribose 1-diphosphate
For diagram 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
Systematic name: 1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase
Links to other databases: BRENDA, EXPASY, KEGG, 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.
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]
Accepted name: anthranilate phosphoribosyltransferase
Reaction: N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-α-D-ribose 1-diphosphate
For diagram 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, 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.
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.
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]
Accepted name: nicotinate-nucleotide diphosphorylase (carboxylating)
Reaction: nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction click here.
Other name(s): quinolinate phosphoribosyltransferase (decarboxylating); quinolinic acid phosphoribosyltransferase; QAPRTase; NAD+ pyrophosphorylase; nicotinate mononucleotide pyrophosphorylase (carboxylating); quinolinic phosphoribosyltransferase
Systematic name: nicotinate-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating)
Comments: This is the first enzyme that prokaryotes and eukaryotes have in common in the production of NAD+ as some prokaryotes use an L-aspartate pathway to produce quinolinate whereas all eukaryotes use tryptophan as the starting material [3].
Links to other databases: BRENDA, EXPASY, KEGG, 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.
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) 851Ð857. [PMID: 16698895]
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, 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.
Accepted name: nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase
Reaction: β-nicotinate D-ribonucleotide + dimethylbenzimidazole = nicotinate + N1-(5-phospho-α-D-ribosyl)-5,6-dimethylbenzimidazole
For diagram click here.
Glossary: α-ribazole 5′-phosphate = N1-(5-phospho-α-D-ribosyl)-5,6-dimethylbenzimidazole
Other name(s): nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase; nicotinate ribonucleotide:benzimidazole (adenine) phosphoribosyltransferase; nicotinate-nucleotide:dimethylbenzimidazole phospho-D-ribosyltransferase; CobT; nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole phosphoribosyltransferase
Systematic name: nicotinate-nucleotide:5,6-dimethylbenzimidazole phospho-D-ribosyltransferase
Comments: Also acts on benzimidazole, and the clostridial enzyme acts on adenine to form 7-α-D-ribosyladenine 5'-phosphate. The product of the reaction, α-ribazole 5′-phosphate, forms part of the corrin-biosynthesis pathway and is a substrate for EC 2.7.8.26, adenosylcobinamide-GDP ribazoletransferase [4]. It can also be dephosphorylated to form α-ribazole by the action of EC 3.1.3.73, α-ribazole phosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37277-76-2
References:
1. Friedmann, H.C. Partial purification and properties of a single displacement trans-N-glycosidase. J. Biol. Chem. 240 (1965) 413-418. [PMID: 14253445]
2. Friedmann, H.C. and Fyfe, J.A. Pseudovitamin B12 biosynthesis. Enzymatic formation of a new adenylic acid, 7-α-D-ribofuranosyladenine 5'-phosphate. J. Biol. Chem. 244 (1969) 1667-1671. [PMID: 5780835]
3. Fyfe, J.A. and Friedmann, H.C. Vitamin B12 biosynthesis. Enzyme studies on the formation of the α-glycosidic nucleotide precursor. J. Biol. Chem. 244 (1969) 1659-1666. [PMID: 4238408]
4. Cameron, B., Blanche, F., Rouyez, M.C., Bisch, D., Famechon, A., Couder, M., Cauchois, L., Thibaut, D., Debussche, L. and Crouzet, J. Genetic analysis, nucleotide sequence, and products of two Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide: dimethylbenzimidazole phosphoribosyltransferase and cobalamin (5′-phosphate) synthase. J. Bacteriol. 173 (1991) 6066-;6073. [PMID: 1917841]
5. Cheong, C.G., Escalante-Semerena, J.C. and Rayment, I. Structural investigation of the biosynthesis of alternative lower ligands for cobamides by nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase from Salmonella enterica. J. Biol. Chem. 276 (2001) 37612-37620. [PMID: 11441022]
6. Cheong, C.G., Escalante-Semerena, J.C. and Rayment, I. Capture of a labile substrate by expulsion of water molecules from the active site of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) from Salmonella enterica. J. Biol. Chem. 277 (2002) 41120-41127. [PMID: 12101181]
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 monophosphate
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, 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]
Accepted name: deoxyuridine phosphorylase
Reaction: 2'-deoxyuridine + phosphate = uracil + 2-deoxy-α-D-ribose 1-phosphate
Other Name(s): deoxyuridine:phosphate deoxy-D-ribosyltransferase; 2'-deoxyuridine:phosphate deoxy-α-D-ribosyltransferase
Systematic name: 2'-deoxyuridine:phosphate 2-deoxy-α-D-ribosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37277-77-3
References:
1. Cihák, A. and Sorm, F. Inhibition by 5-azauracil of the uridine phosphorylase and deoxyuridine phosphorylase activities in a cell-free extract of mouse liver. Biochim. Biophys. Acta 80 (1964) 672-674.
2. Yamada, E.W. The effect of cortisol administration on the activities of uridine and deoxyuridine phosphorylases of normal and regenerating rat liver. Can. J. Biochem. 42 (1964) 317-325.
Accepted name: 1,4-β-D-xylan synthase
Reaction: UDP-D-xylose + [(1→4)-β-D-xylan]n = UDP + [(1→4)-β-D-xylan]n+1
Other name(s): uridine diphosphoxylose-1,4-β-xylan xylosyltransferase; 1,4-β-xylan synthase; xylan synthase; xylan synthetase
Systematic name: UDP-D-xylose:1,4-β-D-xylan 4-β-D-xylosyltransferase
Comments: Formerly EC 2.4.1.72.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37277-73-9
References:
1. Bailey, R.W. and Hassid, W.Z. Xylan synthesis from uridine-diphosphate-D-xylose by particulate preparations from immature corncobs. Proc. Natl. Acad. Sci. USA 56 (1966) 1586-1593.
Accepted name: flavone apiosyltransferase
Reaction: UDP-apiose + 5,7,4'-trihydroxyflavone 7-O-β-D-glucoside = UDP + 5,7,4'-trihydroxyflavone 7-O-[β-D-apiosyl-(1![[arrow right]](../../greek/ARROWR.GIF)
2)-β-D-glucoside]
For diagram click here.
Glossary: apigenin = 5,7,4'-trihydroxyflavone
Other name(s): uridine diphosphoapiose-flavone apiosyltransferase; UDP-apiose:7-O-(β-D-glucosyl)-flavone apiosyltransferase
Systematic name: UDP-apiose:5,4'-dihydroxyflavone 7-O-β-D-glucoside 2"-O-β-D-apiofuranosyltransferase
Comments: 7-O-β-D-Glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37332-49-3
References:
1. Ortmann, R., Sutter, A. and Grisebach, H. Purification and properties of UDPapiose: 7-O-(β-D-glucosyl)-flavone apiosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 289 (1972) 293-302. [PMID: 4650134]
Accepted name: protein xylosyltransferase
Reaction: Transfers a β-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate
Other name(s): UDP-D-xylose:core protein β-D-xylosyltransferase; UDP-D-xylose:core protein xylosyltransferase; UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase; UDP-xylose-core protein β-D-xylosyltransferase; uridine diphosphoxylose-core protein β-xylosyltransferase; uridine diphosphoxylose-protein xylosyltransferase
For diagram click here.
Systematic name: UDP-D-xylose:protein β-D-xylosyltransferase
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 55576-38-0
References:
1. Stoolmiller, A.C., Horwitz, A.L. and Dorfman, A. Biosynthesis of the chondroitin sulfate proteoglycan. Purification and properties of xylosyltransferase. J. Biol. Chem. 247 (1972) 3525-3532. [PMID: 5030630]
2. Götting, C., Kuhn, J., Zahn, R., Brinkmann, T. and Kleesiek, K. Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. J. Mol. Biol. 304 (2000) 517-528. [PMID: 11099377]
Accepted name: dTDP-dihydrostreptose—streptidine-6-phosphate dihydrostreptosyltransferase
Reaction: dTDP-L-dihydrostreptose + streptidine 6-phosphate = dTDP + O-(1→4)-α-L-dihydrostreptosyl-streptidine 6-phosphate
Other name(s): thymidine diphosphodihydrostreptose-streptidine 6-phosphate dihydrostreptosyltransferase
Systematic name: dTDP-L-dihydrostreptose:streptidine-6-phosphate dihydrostreptosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 73699-20-4
References:
1. Kniep, B. and Grisebach, H. Biosynthesis of streptomycin. Purification and properties of a dTDP-L-dihydrostreptose: streptidine-6-phosphate dihydrostreptosyltransferase from Streptomyces griseus.Eur. J. Biochem. 105 (1980) 139-144. [PMID: 6768553]
Accepted name: S-methyl-5'-thioadenosine phosphorylase
Reaction: S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-α-D-ribose 1-phosphate
For diagram click here
Other name(s): 5'-methylthioadenosine nucleosidase; 5'-deoxy-5'-methylthioadenosine phosphorylase; MTA phosphorylase; MeSAdo phosphorylase; MeSAdo/Ado phosphorylase; methylthioadenosine phosphorylase; methylthioadenosine nucleoside phosphorylase; 5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase; S-methyl-5-thioadenosine phosphorylase
Systematic name: S-methyl-5'-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase
Comments: Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 61970-06-7
References:
1. Carteni-Farina, M., Oliva, A., Romeo, G., Napolitano, G., De Rosa, M., Gambacorta, A. and Zappia, V. 5'-Methylthioadenosine phosphorylase from Caldariella acidophila. Purification and properties. Eur. J. Biochem. 101 (1979) 317-324. [PMID: 118001]
2. Garbers, D.L. Demonstration of 5'-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung. Biochim. Biophys. Acta 523 (1978) 82-93. [MPID: 415762]
3. Pegg, A.E. and Williams-Ashman, H.G. Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate. Biochem. J. 115 (1969) 241-247. [PMID: 5378381]
Accepted name: tRNA-guanine transglycosylase
Reaction: (1) [tRNA]-guanine + queuine = [tRNA]-queuine + guanine
(2) [tRNA]-guanine + 7-aminomethyl-7-carbaguanine = [tRNA]-7-aminomethyl-7-carbaguanine + guanine
For diagram click here.
Glossary: preQ1 = 7-aminomethyl-7-carbaguanine
preQ0 = 7-cyano-7-carbaguanine
queuine = base Q = 22-amino-5-({[(1S,4S,5R)-4,5-dihydroxycyclopent-2-en-1-yl]amino}methyl)-1,7-dihydropyrrolo[3,2-e]pyrimidin-4-one
Other name(s): guanine insertion enzyme; tRNA transglycosylase; Q-insertase; queuine transfer ribonucleate ribosyltransferase; transfer ribonucleate glycosyltransferase; tRNA guanine transglycosidase; guanine, queuine-tRNA transglycosylase; queuine tRNA-ribosyltransferase; TGT; [tRNA]-guanine:queuine tRNA-D-ribosyltransferase; transfer ribonucleic acid guanine transglycosylase
Systematic name: tRNA-guanine:queuine tRNA-D-ribosyltransferase
Comments: In eukaryotes, queuine is incorporated into tRNA directly via a base-exchange reaction (replacing guanine) whereas in eubacteria, the queuine precursor preQ1 is incorporated and ultimately modified to queuine [4]. In eubacteria, preQ0 can also be incorporated into undermodified tRNATyr and tRNAAsn containing normal guanine instead of queuine in the first position of the anticodon [2]. This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 72162-89-1
References:
1. Howes, N.K. and Farkas, W.R. Studies with a homogeneous enzyme from rabbit erythrocytes catalyzing the insertion of guanine into tRNA. J. Biol. Chem. 253 (1978) 9082-9087. [PMID: 721832]
2. Okada, N., Noguchi, S., Kasai, H., Shindo-Okada, N., Ohgi, T., Goto, T. and Nishimura, S. Novel mechanism of post-transcriptional modification of tRNA. Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylase reaction. J. Biol. Chem. 254 (1979) 3067-3073. [PMID: 372186]
3. Shindo-Okada, N., Okada, N., Ohgi, T., Goto, T. and Nishimura, S. Transfer ribonucleic acid guanine transglycosylase isolated from rat liver. Biochemistry 19 (1980) 395-400. [PMID: 6986171]
4. Todorov, K.A. and Garcia, G.A. Role of aspartate 143 in Escherichia coli tRNA-guanine transglycosylase: alteration of heterocyclic substrate specificity. Biochemistry 45 (2006) 617-625. [PMID: 16401090]
Accepted name: NAD+ ADP-ribosyltransferase
Reaction: NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
For diagram click here.
Other name(s): poly(ADP-ribose) synthase; ADP-ribosyltransferase (polymerizing); NAD ADP-ribosyltransferase; PARP; PARP-1; NAD+:poly(adenine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyl-transferase (incorrect); NAD+:poly(adenosine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyl-transferase
Systematic name: NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase
Comments: The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 58319-92-9
References:
1. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]
2. Ueda, K., Kawaichi, M. and Hayaishi, O. Poly(ADP-ribose) synthetase. In: Hayaishi, O. and Ueda, K. (Eds.), ADP-Ribosylation Reactions: Biology and Medicine, Academic Press, London, 1982, p. 117-155.
3. Ushiro, H., Yokoyama, Y. and Shizuta, Y. Purification and characterization of poly (ADP-ribose) synthetase from human placenta. J. Biol. Chem. 262 (1987) 2352-2357. [PMID: 2434482]
Accepted name: NAD+—protein-arginine ADP-ribosyltransferase
Reaction: NAD+ + protein L-arginine = nicotinamide + Nω-(ADP-D-ribosyl)-protein-L-arginine
Other name(s): ADP-ribosyltransferase; mono(ADP-ribosyl)transferase; NAD+:L-arginine ADP-D-ribosyltransferase; NAD(P)+-arginine ADP-ribosyltransferase; NAD(P)+:L-arginine ADP-D-ribosyltransferase; mono-ADP-ribosyltransferase; ART; ART1; ART2; ART3; ART4; ART5; ART6; ART7; NAD(P)+—protein-arginine ADP-ribosyltransferase
Systematic name: NAD+:protein-L-arginine ADP-D-ribosyltransferase
Comments: Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nω-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymatic activities. (cf. EC 2.4.2.36 NAD+—diphthamide ADP-ribosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 81457-93-4
References:
1. Moss, J., Stanley, S.J. and Oppenheimer, N.J. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J. Biol. Chem. 254 (1979) 8891-8894. [PMID: 225315]
2. Moss, J., Stanley, S.J. and Watkins, P.A. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255 (1980) 5838-5840. [PMID: 6247348]
3. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]
4. Corda, D. and Di Girolamo, M. Functional aspects of protein mono-ADP-ribosylation. EMBO J. 22 (2003) 1953-1958. [PMID: 12727863]
5. Paone, G., Stevens, L.A., Levine, R.L., Bourgeois, C., Steagall, W.K., Gochuico, B.R. and Moss, J. ADP-ribosyltransferase-specific modification of human neutrophil peptide-1. J. Biol. Chem. 281 (2006) 17054Ð17060. [PMID: 16627471]
Accepted name: dolichyl-phosphate D-xylosyltransferase
Reaction: UDP-D-xylose + dolichyl phosphate = UDP + dolichyl D-xylosyl phosphate
Glossary: dolichol
Systematic name: UDP-D-xylose:dolichyl-phosphate D-xylosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Waechter, C.J., Lucas, J.J. and Lennarz, W.J. Evidence for xylosyl lipids as intermediates in xylosyl transfers in hen oviduct membranes. Biochem. Biophys. Res. Commun. 56 (1974) 343-350. [PMID: 4823870]
Accepted name: dolichyl-xylosyl-phosphate—protein xylosyltransferase
Reaction: dolichyl D-xylosyl phosphate + protein = dolichyl phosphate + D-xylosylprotein
Systematic name: dolichyl-D-xylosyl-phosphate:protein D-xylosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Waechter, C.J., Lucas, J.J. and Lennarz, W.J. Evidence for xylosyl lipids as intermediates in xylosyl transfers in hen oviduct membranes. Biochem. Biophys. Res. Commun. 56 (1974) 343-350. [PMID: 4823870]
Accepted name: indolylacetylinositol arabinosyltransferase
Reaction: UDP-L-arabinose + (indol-3-yl)acetyl-1D-myo-inositol = UDP + (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside
Other name(s): arabinosylindolylacetylinositol synthase; UDP-L-arabinose:indol-3-ylacetyl-myo-inositol L-arabinosyltransferase; UDP-L-arabinose:(indol-3-yl)acetyl-myo-inositol L-arabinosyltransferase
Systematic name: UDP-L-arabinose:(indol-3-yl)acetyl-1D-myo-inositol L-arabinosyltransferase
Comments: The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups. For a diagram showing the biosynthesis of UDP-L-arabinose, click here.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 84720-96-7
References:
1. Corcuera, L.J. and Bandurski, R.S. Biosynthesis of indol-3-yl-acetyl-myo-inositol arabinoside in kernels of Zea mays L. Plant Physiol. 70 (1982) 1664-1666.
Accepted name: flavonol-3-O-glycoside xylosyltransferase
Reaction: UDP-D-xylose + a flavonol 3-O-glycoside = UDP + a flavonol 3-[-D-xylosyl-(1![[arrow right]](../../../../greek/ARROWR.GIF)
2)-β-D-glycoside]
For diagram click here.
Systematic name: UDP-D-xylose:flavonol-3-O-glycoside 2"-O-β-D-xylosyltransferase
Comments: Flavonol 3-O-glucoside, flavonol 3-O-galactoside and, more slowly, rutin, can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 83380-90-9
References:
1. Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv. Apeldoorn. Z. Naturforsch. C: Biosci. 37 (1982) 587-599.
2. Ishikura, N. and Yang, Z.Q. UDP-D-xylose: flavonol 3-O-xylosyltransferase from young leaves of Euonymus alatus f. ciliato-dentatus. Z. Naturforsch. C: Biosci. 46 (1991) 1003-1010.
Accepted name: NAD+—diphthamide ADP-ribosyltransferase
Reaction: NAD+ + peptide diphthamide = nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide
Other name(s): ADP-ribosyltransferase; mono(ADPribosyl)transferase; NAD—diphthamide ADP-ribosyltransferase
Systematic name: NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase
Comments: Diphtheria toxin and some other bacterial toxins catalyse this reaction. The acceptor is a diphthamide residue in elongation factor 2. cf. EC 2.4.2.31 NAD(P)+—protein-arginine ADP-ribosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 52933-21-8
References:
1. Lee, H. and Iglewski, W.J. Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A. Proc. Natl. Acad. Sci. USA 81 (1984) 2703-2707. [PMID: 6326138]
2. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]
Accepted name: NAD+—dinitrogen-reductase ADP-D-ribosyltransferase
Reaction: NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
Other name(s): NAD—azoferredoxin (ADPribose)transferase; NAD—dinitrogen-reductase ADP-D-ribosyltransferase
Systematic name: NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase
Comments: Together with EC 3.2.2.24 (ADP-ribosyl-[dinitrogen reductase] hydrolase), controls the level of activity of EC 1.18.6.1 nitrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 117590-45-1
References:
1. Fitzmaurice, W.P., Saari, L.L., Lowery, R.G., Ludden, P.W. and Roberts, G.P. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum.Mol. Gen. Genet. 218 (1989) 340-347. [PMID: 2506427]
2. Lowery, R.G. and Ludden, P.W. Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum.J. Biol. Chem. 263 (1988) 16714-16719. [PMID: 3141411]
Accepted name: glycoprotein 2-β-D-xylosyltransferase
Reaction: UDP-D-xylose + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine = UDP + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-[β-D-xylosyl-(1→2)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine
For diagram click here.
Other name(s): β1,2-xylosyltransferase
Systematic name: UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase
Comments: Specific for N-linked oligosaccharides (N-glycans).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 141256-56-6
References:
1. Zeng, Y., Bannon, G., Thomas, V.H., Rice, K., Drake, R. and Elbein, A. Purification and specificity of β1,2-xylosyltransferase, an enzyme that contributes to the allergenicity of some plant proteins. J. Biol. Chem. 272 (1997) 31340-31347. [PMID: 9395463]
2. Strasser, R., Mucha, J., Mach, L., Altmann, F., Wilson, I.B., Glössl, J. and Steinkellner, H. Molecular cloning and functional expression of β1,2-xylosyltransferase cDNA from Arabidopsis thaliana. FEBS Lett. 472 (2000) 105-108. [PMID: 10781814]
Accepted name: xyloglucan 6-xylosyltransferase
Reaction: Transfers an α-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an α-(1→6)-D-xylosyl-D-glucose linkage
Other name(s): uridine diphosphoxylose-xyloglucan 6α-xylosyltransferase; xyloglucan 6-α-D-xylosyltransferase
Systematic name: UDP-D-xylose:xyloglucan 1,6-α-D-xylosyltransferase
Comments: In association with EC 2.4.1.168 (xyloglucan 4-glucosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are necessary for this synthesis.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 80238-01-3
References:
1. Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells. Occurrence and some properties of xyloglucan 4-β-D-glucosyltransferase and 6-α-D-xylosyltransferase. J. Biol. Chem. 256 (1981) 11117-11122. [PMID: 6457048]
2. Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells-synthesis of xyloglucan from UDP-glucose and UDP-xylose in the cell-free system. Plant Cell Physiol. 22 (1981) 517-523.
Accepted name: zeatin O-β-D-xylosyltransferase
Reaction: UDP-D-xylose + zeatin = UDP + O-β-D-xylosylzeatin
Glossary: zeatin
Other name(s): uridine diphosphoxylose-zeatin xylosyltransferase; zeatin O-xylosyltransferase
Systematic name: UDP-D-xylose:zeatin O-β-D-xylosyltransferase
Comments: Does not act on UDP-glucose (cf. EC 2.4.1.103 alizarin 2-β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 110541-22-5
References:
1. Turner, J.E., Mok, D.W.S., Mok, M.C. and Shaw, G. Isolation and partial-purification of an enzyme catalyzing the formation of O-xylosylzeatin in Phaseolus vulgaris embryos. Proc. Natl. Acad. Sci. USA 84 (1987) 3714-3717.
Accepted name: xylogalacturonan β-1,3-xylosyltransferase
Reaction: Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a β-1,3-D-xylosyl-D-galactose linkage.
Other name(s): xylogalacturonan xylosyltransferase; XGA xylosyltransferase
Systematic name: UDP-D-xylose:xylogalacturonan β-1,3-xylosyltransferase
Comments: Involved in plant cell wall synthesis. The enzyme from Arabidopsis thaliana also transfers D-xylose from UDP-D-xylose onto oligogalacturonide acceptors. The enzyme did not show significant activity with UDP-glucose, UDP-galactose, or UDP-N-acetyl-D-glucosamine as sugar donors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Jensen, J.K., Sorensen, S.O., Harholt, J., Geshi, N., Sakuragi, Y., Moller, I., Zandleven, J., Bernal, A.J., Jensen, N.B., Sorensen, C., Pauly, M., Beldman, G., Willats, W.G. and Scheller, H.V. Identification of a xylogalacturonan xylosyltransferase involved in pectin biosynthesis in Arabidopsis. Plant Cell 20 (2008) 1289-1302. [PMID: 18460606]
Accepted name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
Reaction: UDP-D-xylose + Glcβ-Ser53-EGF-like domain of bovine factor IX(45-87) = UDP + Xylα(1-3)Glcβ-Ser53-EGF-like domain of bovine factor IX(45-87)
Other name(s): β-glucoside α-1,3-xylosyltransferase
Systematic name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
Comments: The enzyme is involved in the biosynthesis of the Xylα(1-3)Xylα(1-3)Glcβ-1-O-Ser on epidermal growth factor-like domains [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y. and Hase, S. Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1-3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141 (2007) 593-600. [PMID: 17317689]
2. Omichi, K., Aoki, K., Minamida, S. and Hase, S. Presence of UDP-D-xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α 1-3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245 (1997) 143-146. [PMID: 9128735]
Reaction: (1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = -Kdo-(2→4)-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
(2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate
(3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4'-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate
Glossary: lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
4'-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate
lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-[4'-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
Other name(s): undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK, arnT (gene name)
Systematic name: 4-amino-4-deoxy-α-L-2-aminoarabinopyranosyl ditrans,octacis-undecaprenyl phosphate:lipid IVA L-2-aminoarabinopyranosyltransferase
Comments: Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor. J. Biol. Chem. 276 (2001) 43122-43131. [PMID: 11535604]
2. Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm. J. Biol. Chem. 276 (2001) 43132-43144. [PMID: 11535605]
3. Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation. J. Biol. Chem. 276 (2001) 43111-43121. [PMID: 11535603]
4. Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium. Protein Expr. Purif. 46 (2006) 33-39. [PMID: 16226890]
5. Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49 (2010) 29-35. [PMID: 19947657]
Accepted name: S-methyl-5'-thioinosine phosphorylase
Reaction: S-methyl-5'-thioinosine + phosphate = hypoxanthine + S-methyl-5-thio-α-D-ribose 1-phosphate
Other name(s): MTIP; MTI phosphorylase; methylthioinosine phosphorylase
Systematic name: S-methyl-5'-thioinosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase
Comments: No activity with S-methyl-5'-thioadenosine. The catabolism of of 5'-methylthioadenosine in Pseudomonas aeruginosa involves deamination to S-methyl-5'-thioinosine (EC 3.5.4.31, S-methyl-5'-thioadenosine deaminase) and phosphorolysis to hypoxanthine [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Guan, R., Ho, M.C., Almo, S.C. and Schramm, V.L. Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and annotation of a novel enzyme in quorum sensing. Biochemistry 50 (2011) 1247-1254. [PMID: 21197954]
Continued with EC 2.4.99.1 to EC 2.4.99.11
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