The Enzyme Database

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Accepted name: dTDP-4-dehydro-6-deoxyglucose reductase
Reaction: dTDP-α-D-fucopyranose + NAD(P)+ = dTDP-4-dehydro-6-deoxy-α-D-glucose + NAD(P)H + H+
For diagram of dTDP-6-deoxyhexose biosynthesis, click here
Glossary: dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-6-deoxy-α-D-xylo-hexopyranos-4-ulose = thymidine 5′-[3-(6-deoxy--D-xylo-hexopyranosyl-4-ulose) diphosphate]
Other name(s): dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase
Systematic name: dTDP-α-D-fucopyranose:NAD(P)+ oxidoreductase
Comments: The enzymes from the Gram-negative bacteria Aggregatibacter actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens [1,3]. The enzyme from the Gram-positive bacterium Anoxybacillus tepidamans (Geobacillus tepidamans) is involved in activation of fucose for incorporation into the organism’s S-layer [2]. The enzyme from Escherichia coli O52 has a higher catalytic efficiency with NADH than with NADPH [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Yoshida, Y., Nakano, Y., Nezu, T., Yamashita, Y. and Koga, T. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. J. Biol. Chem. 274 (1999) 16933–16939. [DOI] [PMID: 10358040]
2.  Zayni, S., Steiner, K., Pfostl, A., Hofinger, A., Kosma, P., Schaffer, C. and Messner, P. The dTDP-4-dehydro-6-deoxyglucose reductase encoding fcd gene is part of the surface layer glycoprotein glycosylation gene cluster of Geobacillus tepidamans GS5-97T. Glycobiology 17 (2007) 433–443. [DOI] [PMID: 17202151]
3.  Wang, Q., Ding, P., Perepelov, A.V., Xu, Y., Wang, Y., Knirel, Y.A., Wang, L. and Feng, L. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70 (2008) 1358–1367. [DOI] [PMID: 19019146]
[EC created 2001, modified 2013]
Accepted name: acetolactate synthase
Reaction: 2 pyruvate = 2-acetolactate + CO2
For diagram of reaction mechanism, click here
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase
Systematic name: pyruvate:pyruvate acetaldehydetransferase (decarboxylating)
Comments: This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-45-6
1.  Bauerle, R.H., Freundlich, M., Størmer, F.C. and Umbarger, H.E. Control of isoleucine, valine and leucine biosynthesis. II. Endproduct inhibition by valine of acetohydroxy acid synthetase in Salmonella typhimurium. Biochim. Biophys. Acta 92 (1964) 142–149. [PMID: 14243762]
2.  Huseby, N.E., Christensen, T.B., Olsen, B.R. and Størmer, F.C. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure. Eur. J. Biochem. 20 (1971) 209–214. [DOI] [PMID: 5560406]
3.  Størmer, F.C., Solberg, Y. and Hovig, T. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties. Eur. J. Biochem. 10 (1969) 251–260. [DOI] [PMID: 5823101]
4.  Barak, Z., Chipman, D.M. and Gollop, N. Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. J. Bacteriol. 169 (1987) 3750–3756. [DOI] [PMID: 3301814]
[EC created 1972 as EC, transferred 2002 to EC]
Accepted name: sucrose synthase
Reaction: NDP-α-D-glucose + D-fructose = NDP + sucrose
Other name(s): UDPglucose-fructose glucosyltransferase; sucrose synthetase; sucrose-UDP glucosyltransferase; sucrose-uridine diphosphate glucosyltransferase; uridine diphosphoglucose-fructose glucosyltransferase; NDP-glucose:D-fructose 2-α-D-glucosyltransferase
Systematic name: NDP-α-D-glucose:D-fructose 2-α-D-glucosyltransferase (configuration-retaining)
Comments: Although UDP is generally considered to be the preferred nucleoside diphosphate for sucrose synthase, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose [3-9]. Sucrose synthase has a dual role in producing both UDP-glucose (necessary for cell wall and glycoprotein biosynthesis) and ADP-glucose (necessary for starch biosynthesis) [10].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9030-05-1
1.  Avigad, G. and Milner, Y. UDP-glucose:fructose transglucosylase from sugar beet roots. Methods Enzymol. 8 (1966) 341–345.
2.  Cardini, C.E., Leloir, L.F. and Chiriboga, J. The biosynthesis of sucrose. J. Biol. Chem. 214 (1955) 149–155. [PMID: 14367373]
3.  Delmer, D.P. The purification and properties of sucrose synthetase from etiolated Phaseolus aureus seedlings. J. Biol. Chem. 247 (1972) 3822–3828. [PMID: 4624446]
4.  Murata, T., Sugiyama, T., Minamikawa, T. and Akazawa, T. Enzymic mechanism of starch synthesis in ripening rice grains. Mechanism of the sucrose-starch conversion. Arch. Biochem. Biophys. 113 (1966) 34–44. [DOI] [PMID: 5941994]
5.  Nakai, T., Konishi, T., Zhang, X.-Q., Chollet, R., Tonouchi, N., Tsuchida, T., Yoshinaga, F., Mori, H., Sakai, F. and Hayashi, T. An increase in apparent affinity for sucrose of mung bean sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11. Plant Cell Physiol. 39 (1998) 1337–1341. [PMID: 10050318]
6.  Porchia, A.C., Curatti, L. and Salerno, G.L. Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence. Planta 210 (1999) 34–40. [DOI] [PMID: 10592030]
7.  Ross, H.A. and Davies, H.V. Purification and characterization of sucrose synthase from the cotyledons of Vicia fava L. Plant Physiol. 100 (1992) 1008–1013. [PMID: 16653008]
8.  Silvius, J.E. and Snyder, F.W. Comparative enzymic studies of sucrose metabolism in the taproots and fibrous roots of Beta vulgaris L. Plant Physiol. 64 (1979) 1070–1073. [PMID: 16661094]
9.  Tanase, K. and Yamaki, S. Purification and characterization of two sucrose synthase isoforms from Japanese pear fruit. Plant Cell Physiol. 41 (2000) 408–414. [DOI] [PMID: 10845453]
10.  Baroja-Fernández, E., Muñnoz, F.J., Saikusa, T., Rodríguez-López, M., Akazawa, T. and Pozueta-Romero, J. Sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants. Plant Cell Physiol. 44 (2003) 500–509. [PMID: 12773636]
[EC created 1961, modified 2003]
Accepted name: NDP-glucose—starch glucosyltransferase
Reaction: NDP-glucose + [(1→4)-α-D-glucosyl]n = NDP + [(1→4)-α-D-glucosyl]n+1
Other name(s): granule-bound starch synthase; starch synthase II (ambiguous); waxy protein; starch granule-bound nucleoside diphosphate glucose-starch glucosyltransferase; granule-bound starch synthase I; GBSSI; granule-bound starch synthase II; GBSSII; GBSS; NDPglucose-starch glucosyltransferase
Systematic name: NDP-glucose:(1→4)-α-D-glucan 4-α-D-glucosyltransferase
Comments: Unlike EC, glycogen(starch) synthase and EC, starch synthase, which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose. Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. In such mutants, only amylopectin is produced in the endosperm [3] or pollen [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-53-2
1.  Tsai, C.-Y. The function of the waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11 (1974) 83–96. [PMID: 4824506]
2.  Nakamura, T., Vrinten, P., Hayakawa, K. and Ikeda, J. Characterization of a granule-bound starch synthase isoform found in the pericarp of wheat. Plant Physiol. 118 (1998) 451–459. [PMID: 9765530]
3.  Fujita, N. and Taira, T. A 56-kDa protein is a novel granule-bound starch synthase existing in the pericarps, aleurone layers, and embryos of immature seed in diploid wheat (Triticum monococcum L.). Planta 207 (1998) 125–132. [DOI] [PMID: 9951718]
4.  Murai, J., Taira, T. and Ohta, D. Isolation and characterization of the three Waxy genes encoding the granule-bound starch synthase in hexaploid wheat. Gene 234 (1999) 71–79. [DOI] [PMID: 10393240]
5.  Nelson, O.E. The waxy locus in maize. II The location of the controlling element alleles. Genetics 60 (1968) 507–524. [PMID: 17248421]
[EC created 2005]
Accepted name: α,α-trehalose synthase
Reaction: NDP-α-D-glucose + D-glucose = α,α-trehalose + NDP
Glossary: NDP = a nucleoside diphosphate
Other name(s): trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase
Systematic name: NDP-α-D-glucose:D-glucose 1-α-D-glucosyltransferase
Comments: Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-α-D-glucose to the same extent [2,3], that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose [1] and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Qu, Q., Lee, S.J. and Boos, W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 279 (2004) 47890–47897. [DOI] [PMID: 15364950]
2.  Ryu, S.I., Park, C.S., Cha, J., Woo, E.J. and Lee, S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 329 (2005) 429–436. [DOI] [PMID: 15737605]
3.  Nobre, A., Alarico, S., Fernandes, C., Empadinhas, N. and da Costa, M.S. A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT. J. Bacteriol. 190 (2008) 7939–7946. [DOI] [PMID: 18835983]
4.  Kouril, T., Zaparty, M., Marrero, J., Brinkmann, H. and Siebers, B. A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway. Arch. Microbiol. 190 (2008) 355–369. [DOI] [PMID: 18483808]
[EC created 2008, modified 2013]
Accepted name: glucosyl-3-phosphoglycerate synthase
Reaction: NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate
Other name(s): GpgS protein; GPG synthase; glucosylphosphoglycerate synthase
Systematic name: NDP-glucose:3-phospho-D-glycerate 2-α-D-glucosyltransferase
Comments: The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by EC glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor [1]. The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate [2]. This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Costa, J., Empadinhas, N. and da Costa, M.S. Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina. J. Bacteriol. 189 (2007) 1648–1654. [DOI] [PMID: 17189358]
2.  Costa, J., Empadinhas, N., Goncalves, L., Lamosa, P., Santos, H. and da Costa, M.S. Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii. J. Bacteriol. 188 (2006) 1022–1030. [DOI] [PMID: 16428406]
3.  Empadinhas, N., Albuquerque, L., Mendes, V., Macedo-Ribeiro, S. and da Costa, M.S. Identification of the mycobacterial glucosyl-3-phosphoglycerate synthase. FEMS Microbiol. Lett. 280 (2008) 195–202. [DOI] [PMID: 18221489]
4.  Pereira, P.J., Empadinhas, N., Albuquerque, L., Sa-Moura, B., da Costa, M.S. and Macedo-Ribeiro, S. Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis. PLoS One 3:e3748 (2008). [DOI] [PMID: 19015727]
5.  Gest, P., Kaur, D., Pham, H.T., van der Woerd, M., Hansen, E., Brennan, P.J., Jackson, M. and Guerin, M.E. Preliminary crystallographic analysis of GpgS, a key glucosyltransferase involved in methylglucose lipopolysaccharide biosynthesis in Mycobacterium tuberculosis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1121–1124. [DOI] [PMID: 19052364]
6.  Kaur, D., Pham, H., Larrouy-Maumus, G., Riviere, M., Vissa, V., Guerin, M.E., Puzo, G., Brennan, P.J. and Jackson, M. Initiation of methylglucose lipopolysaccharide biosynthesis in mycobacteria. PLoS One 4:e544 (2009). [DOI] [PMID: 19421329]
[EC created 2011]
Accepted name: glucosylglycerate synthase
Reaction: ADP-glucose + D-glycerate = 2-O-(α-D-glucopyranosyl)-D-glycerate + ADP
Other name(s): Ggs (gene name)
Systematic name: ADP-glucose:D-glycerate 2-α-D-glucosyltransferase
Comments: Persephonella marina possesses two enzymic systems for the synthesis of glucosylglycerate. The first one is a single-step pathway in which glucosylglycerate synthase catalyses the synthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate in one-step from ADP-glucose and D-glycerate. The second system is a two-step pathway in which EC (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of NDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by EC (glucosyl-3-phosphoglycerate phosphatase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Fernandes, C., Empadinhas, N. and da Costa, M.S. Single-step pathway for synthesis of glucosylglycerate in Persephonella marina. J. Bacteriol. 189 (2007) 4014–4019. [DOI] [PMID: 17369297]
2.  Fernandes, C., Mendes, V., Costa, J., Empadinhas, N., Jorge, C., Lamosa, P., Santos, H. and da Costa, M.S. Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis. J. Bacteriol. 192 (2010) 1624–1633. [DOI] [PMID: 20061481]
[EC created 2011]
Accepted name: NDP-glycosyltransferase
Reaction: an NDP-glycose + an acceptor = a glycosylated acceptor + NDP
Other name(s): yjiC (gene name)
Systematic name: NDP-glycose:acceptor glycosyltransferase
Comments: The enzyme, characterized from the bacterium Bacillus licheniformis DSM-13, is an extremely promiscuous glycosyltransferase. It can accept ADP-, GDP-, CDP-, TDP-, or UDP-activated glycose molecules as donors, and can glycosylate a large number of substrates, catalysing O-, N-, or S-glycosylation. While D-glucose is the primarily reported sugar being transferred, the enzyme has been shown to transfer D-galactose, 2-deoxy-D-glucose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, L-fucose, L-rhamnose, D-glucuronate, and D-viosamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Pandey, R.P., Parajuli, P., Koirala, N., Park, J.W. and Sohng, J.K. Probing 3-hydroxyflavone for in vitro glycorandomization of flavonols by YjiC. Appl. Environ. Microbiol. 79 (2013) 6833–6838. [DOI] [PMID: 23974133]
2.  Pandey, R.P., Gurung, R.B., Parajuli, P., Koirala, N., Tuoi le, T. and Sohng, J.K. Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids. Carbohydr. Res. 393 (2014) 26–31. [DOI] [PMID: 24893262]
3.  Pandey, R.P., Parajuli, P., Shin, J.Y., Lee, J., Lee, S., Hong, Y.S., Park, Y.I., Kim, J.S. and Sohng, J.K. Enzymatic biosynthesis of novel resveratrol glucoside and glycoside derivatives. Appl. Environ. Microbiol. 80 (2014) 7235–7243. [DOI] [PMID: 25239890]
4.  Parajuli, P., Pandey, R.P., Koirala, N., Yoon, Y.J., Kim, B.G. and Sohng, J.K. Enzymatic synthesis of epothilone A glycosides. AMB Express 4:31 (2014). [DOI] [PMID: 24949266]
5.  Pandey, R.P., Parajuli, P., Gurung, R.B. and Sohng, J.K. Donor specificity of YjiC glycosyltransferase determines the conjugation of cytosolic NDP-sugar in in vivo glycosylation reactions. Enzyme Microb. Technol. 91 (2016) 26–33. [DOI] [PMID: 27444326]
6.  Bashyal, P., Thapa, S.B., Kim, T.S., Pandey, R.P. and Sohng, J.K. Exploring the nucleophilic N- and S-glycosylation capacity of Bacillus licheniformis YjiC enzyme. J. Microbiol. Biotechnol. 30 (2020) 1092–1096. [DOI] [PMID: 32238768]
[EC created 2021]
Accepted name: deoxycytidine kinase
Reaction: NTP + deoxycytidine = NDP + dCMP
Other name(s): deoxycytidine kinase (phosphorylating); 2′-deoxycytidine kinase; Ara-C kinase; arabinofuranosylcytosine kinase; deoxycytidine-cytidine kinase
Systematic name: NTP:deoxycytidine 5′-phosphotransferase
Comments: Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9039-45-6
1.  Durham, J.P. and Ives, D.H. Deoxycytidine kinase. II. Purification and general properties of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2276–2284. [PMID: 5442271]
2.  Ives, D.H. and Durham, J.P. Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2285–2294. [PMID: 5462538]
3.  Kessel, D. Properties of deoxycytidine kinase partially purified from L1210 cells. J. Biol. Chem. 243 (1968) 4739–4744. [PMID: 5687717]
4.  Momparler, R.L. and Fischer, G.A. Mammalian deoxynucleoside kinase. I. Deoxycytidine kinase: purification, properties, and kinetic studies with cytosine arabinoside. J. Biol. Chem. 243 (1968) 4298–4304. [PMID: 5684726]
[EC created 1972]
Accepted name: nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase
Reaction: nucleoside triphosphate + α-D-aldose 1-phosphate = diphosphate + NDP-hexose
Other name(s): NDP hexose pyrophosphorylase; hexose 1-phosphate nucleotidyltransferase; hexose nucleotidylating enzyme; nucleoside diphosphohexose pyrophosphorylase; hexose-1-phosphate guanylyltransferase; GTP:α-D-hexose-1-phosphate guanylyltransferase; GDP hexose pyrophosphorylase; guanosine diphosphohexose pyrophosphorylase; nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase; NTP:hexose-1-phosphate nucleotidyltransferase
Systematic name: NTP:α-D-aldose-1-phosphate nucleotidyltransferase
Comments: In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-26-5
1.  Verachtert, H., Rodriguez, P., Bass, S.T. and Hansen, R.G. Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues. J. Biol. Chem. 241 (1966) 2007–2013. [PMID: 5946626]
2.  Hansen, R.G., Verachtert, H., Rodriguez, P. and Bass, S.T. GDP-hexose pyrophosphorylase from liver. Methods Enzymol. 8 (1966) 269–271.
[EC created 1972, modified 2004 (EC created 1972, incorporated 2004)]
Accepted name: aldose-1-phosphate nucleotidyltransferase
Reaction: NDP + α-D-aldose 1-phosphate = phosphate + NDP-aldose
For diagram of UDP-L-arabinose, UDP-galacturonate and UDP-xylose biosynthesis, click here
Other name(s): sugar-1-phosphate nucleotidyltransferase; NDPaldose phosphorylase; glucose 1-phosphate inosityltransferase; NDP sugar phosphorylase; nucleoside diphosphosugar phosphorylase; sugar phosphate nucleotidyltransferase; nucleoside diphosphate sugar:orthophosphate nucleotidyltransferase; sugar nucleotide phosphorylase; NDP:aldose-1-phosphate nucleotidyltransferase
Systematic name: NDP:α-D-aldose-1-phosphate nucleotidyltransferase
Comments: The enzyme works on a variety of α-D-aldose 1-phosphates and β-L-aldose 1-phosphates (which have the same anomeric configuration as the former; see 2-Carb-6.2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-61-8
1.  Cabib, E., Carminatti, H. and Woyskovsky, N.M. Phosphorolysis of the pyrophosphate bond of sugar nucleotides. II. Purification and properties of the enzyme. J. Biol. Chem. 240 (1965) 2114–2121. [PMID: 14299635]
[EC created 1972, modified 1986]
Accepted name: ATP adenylyltransferase
Reaction: ADP + ATP = phosphate + P1,P4-bis(5′-adenosyl) tetraphosphate
Other name(s): bis(5′-nucleosyl)-tetraphosphate phosphorylase (NDP-forming); diadenosinetetraphosphate αβ-phosphorylase; adenine triphosphate adenylyltransferase; diadenosine 5′,5′′′-P1,P4-tetraphosphate αβ-phosphorylase (ADP-forming); dinucleoside oligophosphate αβ-phosphorylase
Systematic name: ADP:ATP adenylyltransferase
Comments: GTP and adenosine tetraphosphate can also act as adenylyl acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96697-71-1
1.  Guranowski, A. and Blanquet, S. Phosphorolytic cleavage of diadenosine 5′,5′′′-P1,P4-tetraphosphate. Properties of homogeneous diadenosine 5′,5′′′- P1,P4-tetraphosphate αβ-phosphorylase from Saccharomyces cerevisiae. J. Biol. Chem. 260 (1985) 3542–3547. [PMID: 2982863]
[EC created 1986]
Accepted name: apyrase
Reaction: a nucleoside 5′-triphosphate + 2 H2O = a nucleoside 5′-phosphate + 2 phosphate (overall reaction)
(1a) a nucleoside 5′-triphosphate + H2O = a nucleoside 5′-diphosphate + phosphate
(1b) a nucleoside 5′-diphosphate + H2O = a nucleoside 5′-phosphate + phosphate
Other name(s): ATP-diphosphatase (ambiguous); adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]
Systematic name: nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Comments: Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9000-95-7
1.  Krishnan, P.S. Apyrase, pyrophosphatase and metaphosphatase of Penicillium chrysogenum. Arch. Biochem. Biophys. 37 (1952) 224–234. [DOI] [PMID: 14953432]
2.  Liébecq, C., Lallemand, A. and Degueldre-Guillaume, M.-J. [Partial purification and properties of potato apyrase.] Bull. Soc. Chim. Biol. 45 (1963) 573–594. [PMID: 13930517] (in French)
3.  Chen, Y.R., Datta, N. and Roux, S.J. Purification and partial characterization of a calmodulin-stimulated nucleoside triphosphatase from pea nuclei. J. Biol. Chem. 262 (1987) 10689–10694. [PMID: 3038893]
4.  Christoforidis, S., Papamarcaki, T., Galaris, D., Kellner, R. and Tsolas, O. Purification and properties of human placental ATP diphosphohydrolase. Eur. J. Biochem. 234 (1995) 66–74. [DOI] [PMID: 8529670]
5.  Wang, T.F. and Guidotti, G. CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J. Biol. Chem. 271 (1996) 9898–9901. [DOI] [PMID: 8626624]
6.  Gao, X.D., Kaigorodov, V. and Jigami, Y. YND1, a homologue of GDA1, encodes membrane-bound apyrase required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae. J. Biol. Chem. 274 (1999) 21450–21456. [DOI] [PMID: 10409709]
7.  Xu, W., Jones, C.R., Dunn, C.A. and Bessman, M.J. Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily. J. Bacteriol. 186 (2004) 8380–8384. [DOI] [PMID: 15576788]
[EC created 1961, modified 1976, modified 2000, modified 2013]
Accepted name: nucleoside diphosphate phosphatase
Reaction: a nucleoside diphosphate + H2O = a nucleoside phosphate + phosphate
Other name(s): nucleoside-diphosphatase; thiaminpyrophosphatase; UDPase; inosine diphosphatase; adenosine diphosphatase; IDPase; ADPase; adenosinepyrophosphatase; guanosine diphosphatase; guanosine 5′-diphosphatase; inosine 5′-diphosphatase; uridine diphosphatase; uridine 5′-diphosphatase; type B nucleoside diphosphatase; GDPase; CDPase; nucleoside 5′-diphosphatase; type L nucleoside diphosphatase; NDPase; nucleoside diphosphate phosphohydrolase
Systematic name: nucleoside-diphosphate phosphohydrolase
Comments: The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate. Specificity depends on species and isoform.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-69-4
1.  Gibson, D.M., Ayengar, P. and Sanadi, D.R. A phosphatase specific for nucleoside diphosphates. Biochim. Biophys. Acta 16 (1955) 536–538. [DOI] [PMID: 14389272]
2.  Horecker, B.L., Hurwitz, J. and Heppel, L.A. The synthesis of ribose 5-pyrophosphate and ribose 5-triphosphate. J. Am. Chem. Soc. 79 (1957) 701–702.
3.  Yeung, G., Mulero, J.J., McGowan, D.W., Bajwa, S.S. and Ford, J.E. CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry 39 (2000) 12916–12923. [DOI] [PMID: 11041856]
4.  Failer, B.U., Braun, N. and Zimmermann, H. Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J. Biol. Chem. 277 (2002) 36978–36986. [DOI] [PMID: 12167635]
5.  Uccelletti, D., O'Callaghan, C., Berninsone, P., Zemtseva, I., Abeijon, C. and Hirschberg, C.B. ire-1-dependent transcriptional up-regulation of a lumenal uridine diphosphatase from Caenorhabditis elegans. J. Biol. Chem. 279 (2004) 27390–27398. [DOI] [PMID: 15102851]
[EC created 1961]

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