EC 2.4.1.1 to EC 2.4.1.50
EC 2.4.1.51 to EC 2.4.1.100
EC 2.4.1.101 to EC 2.4.1.150
EC 2.4.1.151 to EC 2.4.1.200
EC 2.4.1.201 to EC 2.4.1.250
Accepted name: GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 4-β-mannosyltransferase
Reaction: GDP-mannose + GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol = GDP + D-Man-β-(1→4)- GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol
For diagram of reaction click here.
Other name(s): GumI
Systematic name: GDP-mannose:GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 4-β-mannosyltransferase
Comments: The enzyme is involved in the biosynthesis of the exopolysaccharide xanthan.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Katzen, F., Ferreiro, D.U., Oddo, C.G., Ielmini, M.V., Becker, A., Puhler, A. and Ielpi, L. Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence. J. Bacteriol. 180 (1998) 1607-1617. [PMID: 9537354]
2. Ielpi, L., Couso, R.O. and Dankert, M.A. Sequential assembly and polymerization of the polyprenol-linked pentasaccharide repeating unit of the xanthan polysaccharide in Xanthomonas campestris. J. Bacteriol. 175 (1993) 2490-2500. [PMID: 7683019]
3. Kim, S.Y., Kim, J.G., Lee, B.M. and Cho, J.Y. Mutational analysis of the gum gene cluster required for xanthan biosynthesis in Xanthomonas oryzae pv oryzae. Biotechnol. Lett. 31 (2009) 265-270. [PMID: 18854951]
Accepted name: GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase
Reaction: GDP-mannose + D-Glc-β-(1→4)-Glc-α-1-diphospho-ditrans,octacis-undecaprenol = GDP + D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol
For diagram of reaction click here.
Other name(s): GumH; AceA; α1,3-mannosyltransferase AceA
Systematic name: GDP-mannose:D-Glc-β-(1→4)-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase
Comments: In the bacterium Gluconacetobacter xylinus (previously known as Acetobacter xylinum) the enzyme is involved in the biosynthesis of the exopolysaccharide acetan [1]. In Xanthomonas campestris the enzyme is involved in the biosynthesis of the exopolysaccharide xanthan [5].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Geremia, R.A., Roux, M., Ferreiro, D.U., Dauphin-Dubois, R., Lellouch, A.C. and Ielpi, L. Expression and biochemical characterisation of recombinant AceA, a bacterial α-mannosyltransferase. Mol. Gen. Genet. 261 (1999) 933-940. [PMID: 10485283]
2. Abdian, P.L., Lellouch, A.C., Gautier, C., Ielpi, L. and Geremia, R.A. Identification of essential amino acids in the bacterial α-mannosyltransferase aceA. J. Biol. Chem. 275 (2000) 40568-40575. [PMID: 11001941]
3. Petroni, E.A. and Ielpi, L. Isolation and nucleotide sequence of the GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase gene from Acetobacter xylinum. J. Bacteriol. 178 (1996) 4814-4821. [PMID: 8759843]
4. Lellouch, A.C., Watt, G.M., Geremia, R.A. and Flitsch, S.L. Phytanyl-pyrophosphate-linked substrate for a bacterial α-mannosyltransferase. Biochem. Biophys. Res. Commun. 272 (2000) 290-292. [PMID: 10872841]
5. Katzen, F., Ferreiro, D.U., Oddo, C.G., Ielmini, M.V., Becker, A., Puhler, A. and Ielpi, L. Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence. J. Bacteriol. 180 (1998) 1607-1617. [PMID: 9537354]
Accepted name: baicalein 7-O-glucuronosyltransferase
Reaction: UDP-D-glucuronate + baicalein = UDP + baicalin
Glossary: baicalin = 5,6,7-trihydroxyflavone-7-O-β-D-glucuronate = 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl β-D-glucupyranosiduronic acid
baicalein = 5,6,7-trihydroxyflavone = 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one
wogonin = 5,7-dihydroxy-8-methoxyflavone = 5,7-dihydroxy-8-methoxy-2-phenyl-4H-chromen-4-one
scutellarein = 4,5,6,7-tetrahydroxyflavone-7-O-β-D-glucoronate = 5,6,7-trihydroxy-2-(4-hydroxyphenyl)chromen-4-one
Other name(s): UBGAT
Systematic name: UDP-D-glucuronate:5,6,7-trihydroxyflavone 7-O-glucuronosyltransferase
Comments: The enzyme is specific for UDP-D-glucuronate as a sugar donor and flavones with substitution ortho- to the 7-OH group such as baicalein (6-OH), scutellarein (6-OH) and wogonin (8-OMe).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Nagashima, S., Hirotani, M. and Yoshikawa, T. Purification and characterization of UDP-glucuronate: baicalein 7-O-glucuronosyltransferase from Scutellaria baicalensis Georgi. cell suspension cultures. Phytochemistry 53 (2000) 533-538. [PMID: 10724177]
Accepted name: cyanidin-3-O-glucoside 2-O-glucuronosyltransferase
Reaction: UDP-D-glucuronate + cyanidin 3-O-β-D-glucoside = UDP + cyanidin 3-O-(2-O-β-D-glucuronosyl)-β-D-glucoside
Other name(s): BpUGT94B1; UDP-glucuronic acid:anthocyanin glucuronosyltransferase; UDP-glucuronic acid:anthocyanidin 3-glucoside 2'-O-β-glucuronosyltransferase; BpUGAT
Systematic name: UDP-D-glucuronate:cyanidin-3-O-β-glucoside 2-O-β-glucuronosyltransferase
Comments: The enzyme is highly specific for cyanidin 3-O-glucosides and UDP-D-glucuronate. Involved in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Sawada, S., Suzuki, H., Ichimaida, F., Yamaguchi, M.A., Iwashita, T., Fukui, Y., Hemmi, H., Nishino, T. and Nakayama, T. UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers. Enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis. J. Biol. Chem. 280 (2005) 899-906. [PMID: 15509561]
2. Osmani, S.A., Bak, S., Imberty, A., Olsen, C.E. and Møller, B.L. Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-specific mutagenesis and biochemical analyses. Plant Physiol. 148 (2008) 1295-1308. [PMID: 18829982]
Accepted name: protein O-GlcNAc transferase
Reaction: (1) UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine
(2) UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-threonine
Other name(s): O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; protein O-linked β-N-acetylglucosamine transferase
Systematic name: UDP-N-acetyl-D-glucosamine:protein-O-β-N-acetyl-D-glucosaminyl transferase
Comments: Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Banerjee, S., Robbins, P.W. and Samuelson, J. Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum. Glycobiology 19 (2009) 331-336. [PMID: 18948359]
2. Clarke, A.J., Hurtado-Guerrero, R., Pathak, S., Schuttelkopf, A.W., Borodkin, V., Shepherd, S.M., Ibrahim, A.F. and van Aalten, D.M. Structural insights into mechanism and specificity of O-GlcNAc transferase. EMBO J. 27 (2008) 2780-2788. [PMID: 18818698]
3. Rao, F.V., Dorfmueller, H.C., Villa, F., Allwood, M., Eggleston, I.M. and van Aalten, D.M. Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25 (2006) 1569-1578. [PMID: 16541109]
4. Haltiwanger, R.S., Blomberg, M.A. and Hart, G.W. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase. J. Biol. Chem. 267 (1992) 9005-9013. [PMID: 1533623]
5. Lubas, W.A., Frank, D.W., Krause, M. and Hanover, J.A. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9316-9324. [PMID: 9083068]
6. Lazarus, M.B., Nam, Y., Jiang, J., Sliz, P. and Walker, S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469 (2011) 564-567. [PMID: 21240259]
Accepted name: Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Glc-α-(1→2)-D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of reaction click here.
Other name(s): ALG10
Systematic name: dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,2-glucosyltransferase
Comments: This enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch.
References:
1. Burda, P. and Aebi, M. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8 (1998) 455-462. [PMID: 9597543]
Accepted name: GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase
Reaction: GDP-D-mannose + D-Man-α-(1→3)-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol
For diagram of reaction click here.
Other name(s): Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous)
Systematic name: GDP-D-mannose:D-Man-α-(1→3)-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase
Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900-11912. [PMID: 19282279]
2. O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593-9603. [PMID: 16878994]
Accepted name: Dol-P-Man:Man5GlcNAc2-PP-Dol α-1,3-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of reaction click here.
Other name(s): Man5GlcNAc2-PP-Dol mannosyltransferase; ALG3; dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase; Not56-like protein; Alg3 α-1,3-mannosyl transferase
Systematic name: dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-mannosyltransferase
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Sharma, C.B., Knauer, R. and Lehle, L. Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase. Biol. Chem. 382 (2001) 321-328. [PMID: 11308030]
2. Cipollo, J.F. and Trimble, R.B. The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Δalg9 mutant reveals a regulatory role for the Alg3p α1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. J. Biol. Chem. 275 (2000) 4267-4277. [PMID: 10660594]
Accepted name: Dol-P-Man:Man6GlcNAc2-PP-Dol α-1,2-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of reaction click here.
Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase
Systematic name: dolichyl β-D-mannosyl phosphate: D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,2-mannosyltransferase
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues Ð the addition of α-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G., Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910-917. [PMID: 19451548]
2. Cipollo, J.F. and Trimble, R.B. The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Δalg9 mutant reveals a regulatory role for the Alg3p α1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. J. Biol. Chem. 275 (2000) 4267-4277. [PMID: 10660594]
3. Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156-1163. [PMID: 15987956]
Accepted name: Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of reaction click here.
Other name(s): ALG12; ALG12 mannosyltransferase; ALG12 α1,6mannosyltransferase; dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase; dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl α6-mannosyltransferase; EBS4
Systematic name: dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,6-mannosyltransferase
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156-1163. [PMID: 15987956]
2. Hong, Z., Jin, H., Fitchette, A.C., Xia, Y., Monk, A.M., Faye, L. and Li, J. Mutations of an α1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis. Plant Cell 21 (2009) 3792-3802. [PMID: 20023196]
3. Cipollo, J.F. and Trimble, R.B. The Saccharomyces cerevisiae alg12δ mutant reveals a role for the middle-arm α1,2Man- and upper-arm α1,2Manα1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus. Glycobiology 12 (2002) 749-762. [PMID: 12460943]
4. Grubenmann, C.E., Frank, C.G., Kjaergaard, S., Berger, E.G., Aebi, M. and Hennet, T. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum. Mol. Genet. 11 (2002) 2331-2339. [PMID: 12217961]
Accepted name: Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of reaction click here.
Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase
Systematic name: dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,2-mannosyltransferase
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues: the addition of α-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G., Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (0) 910-917. [PMID: 19451548]
2. Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156-1163. [PMID: 15987956]
Accepted name: soyasapogenol glucuronosyltransferase
Reaction: UDP-glucuronate + soyasapogenol B = UDP + soyasapogenol B 3-O-D-glucuronide
For diagram of reaction click here.
Other name(s): UGASGT
Systematic name: UDP-D-glucuronate:soyasapogenol 3-O-D-glucuronosyltransferase
Comments: Requires a divalent ion, Mg2+ better than Mn2+, better than Ca2+. Also acts on soysapogenol A and E.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Kurosawa, Y., Takahara, H. and Shiraiwa, M. UDP-glucuronic acid:soyasapogenol glucuronosyltransferase involved in saponin biosynthesis in germinating soybean seeds. Planta 215 (2002) 620-629. [PMID: 12172845]
Accepted name: abscisate β-glucosyltransferase
Reaction: UDP-D-glucose + abscisate = UDP + β-D-glucopyranosyl abscisate
For diagram of reaction click here.
Other name(s): ABA-glucosyltransferase; ABA-GTase; AOG
Systematic name: UDP-D-glucose:abscisate β-D-glucosyltransferase
Comments: The enzyme acts better on (S)-2-trans-abscisate than the natural (S)-2-cis isomer, abscisate, or its enantiomer, the (R)-2-cis isomer.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Xu, Z.J., Nakajima, M., Suzuki, Y. and Yamaguchi, I. Cloning and characterization of the abscisic acid-specific glucosyltransferase gene from adzuki bean seedlings. Plant Physiol. 129 (2002) 1285-1295. [PMID: 12114582]
Accepted name: D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 2-β-glucuronyltransferase
Reaction: UDP-glucuronate + D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol = UDP + D-GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol
For diagram of reaction click here.
Other name(s): GumK
Systematic name: UDP-glucuronate:D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol β-1,2-glucuronyltransferase
Comments: The enzyme is involved in the biosynthesis of the exopolysaccharides xanthan (in the bacterium Xanthomonas campestris) and acetan (in the bacterium Gluconacetobacter xylinus).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Katzen, F., Ferreiro, D.U., Oddo, C.G., Ielmini, M.V., Becker, A., Puhler, A. and Ielpi, L. Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence. J. Bacteriol. 180 (1998) 1607-1617. [PMID: 9537354]
2. Ielpi, L., Couso, R.O. and Dankert, M.A. Sequential assembly and polymerization of the polyprenol-linked pentasaccharide repeating unit of the xanthan polysaccharide in Xanthomonas campestris. J. Bacteriol. 175 (1993) 2490-2500. [PMID: 7683019]
3. Kim, S.Y., Kim, J.G., Lee, B.M. and Cho, J.Y. Mutational analysis of the gum gene cluster required for xanthan biosynthesis in Xanthomonas oryzae pv oryzae. Biotechnol. Lett. 31 (2009) 265-270. [PMID: 18854951]
4. Barreras, M., Bianchet, M.A. and Ielpi, L. Crystallization and preliminary crystallographic characterization of GumK, a membrane-associated glucuronosyltransferase from Xanthomonas campestris required for xanthan polysaccharide synthesis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 880-883. [PMID: 16946469]
5. Barreras, M., Salinas, S.R., Abdian, P.L., Kampel, M.A. and Ielpi, L. Structure and mechanism of GumK, a membrane-associated glucuronosyltransferase. J. Biol. Chem. 283 (2008) 25027-25035. [PMID: 18596046]
6. Vojnov, A.A., Bassi, D.E., Daniels, M.J. and Dankert, M.A. Biosynthesis of a substituted cellulose from a mutant strain of Xanthomonas campestris. Carbohydr. Res. 337 (2002) 315-326. [PMID: 11841812]
7. Barreras, M., Abdian, P.L. and Ielpi, L. Functional characterization of GumK, a membrane-associated β-glucuronosyltransferase from Xanthomonas campestris required for xanthan polysaccharide synthesis. Glycobiology 14 (2004) 233-241. [PMID: 14736729]
Accepted name: Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of reaction click here.
Other name(s): ALG8
Systematic name: dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Comments: The successive addition of three glucose residues by EC 2.4.1.267 (Dol-P-Glc:Man9GlcNAc2-PP-Dol -1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol 1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Stagljar, I., te Heesen, S. and Aebi, M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. USA 91 (1994) 5977-5981. [PMID: 8016100]
2. Runge, K.W. and Robbins, P.W. A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J. Biol. Chem. 261 (1986) 15582-15590. [PMID: 3536907]
3. Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J. Biol. Chem. 278 (2003) 9962-9971. [PMID: 12480927]
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 3.1.3.85 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, CAS registry number:
References:
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. [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. [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. [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 (2008) e3748. [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. [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 (2009) e544. [PMID: 19421329]
Accepted name: Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of reaction click here.
Other name(s): ALG6
Systematic name: dolichyl β-D-glucosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Comments: The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol -1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol 1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology 6 (1996) 493-498. [PMID: 8877369]
2. Runge, K.W., Huffaker, T.C. and Robbins, P.W. Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway. J. Biol. Chem. 259 (1984) 412-417. [PMID: 6423630]
3. Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic. Hum. Mutat. 22 (2003) 420-421. [PMID: 14517965]
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 enzymatic 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 2.4.1.266 (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 3.1.3.85 (glucosyl-3-phosphoglycerate phosphatase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
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. [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. [PMID: 20061481]
Accepted name: mannosylglycerate synthase
Reaction: GDP-mannose + D-glycerate = GDP + 2-O-(α-D-mannopyranosyl)-D-glycerate
Systematic name: GDP-mannose:D-glycerate 2-α-D-mannosyltransferase
Comments: Rhodothermus marinus can also form mannosylglycerate via a two-step pathway catalysed by EC 2.4.1.217 (mannosyl-3-phosphoglycerate synthase) and EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase) [1]. Depending on experimental conditions mannosylglycerate synthase is more or less specific for the GDP-mannose and D-glycerate [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Martins, L.O., Empadinhas, N., Marugg, J.D., Miguel, C., Ferreira, C., da Costa, M.S. and Santos, H. Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase. J. Biol. Chem. 274 (1999) 35407-35414. [PMID: 10585410]
2. Flint, J., Taylor, E., Yang, M., Bolam, D.N., Tailford, L.E., Martinez-Fleites, C., Dodson, E.J., Davis, B.G., Gilbert, H.J. and Davies, G.J. Structural dissection and high-throughput screening of mannosylglycerate synthase. Nat. Struct. Mol. Biol. 12 (2005) 608-614. [PMID: 15951819]
Accepted name: mannosylglucosyl-3-phosphoglycerate synthase
Reaction: GDP-mannose + 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate = GDP + 2-O-[2-O-(α-D-mannopyranosyl)-α-D-glucopyranosyl]-3-phospho-D-glycerate
Other name(s): MggA
Systematic name: GDP-mannose:2-O-(α-D-glucosyl)-3-phospho-D-glycerate 2-O-α-D-mannosyltransferase
Comments: The enzyme is involved in synthesis of 2-[2-O-(α-D-mannopranosyl)-α-D-glucopyranosyl]-D-glycerate. Petrotoga miotherma and Petrotoga mobilis accumulate this compound in response to water stress imposed by salt.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. 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. [PMID: 20061481]
Accepted name: crocetin glucosyltransferase
Reaction: (1) UDP-glucose + crocetin = UDP + β-D-glucosyl crocetin
(2) UDP-glucose + β-D-glucosyl crocetin = UDP + bis(β-D-glucosyl) crocetin
(3) UDP-glucose + β-D-gentiobiosyl crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
For diagram of reaction click here.
Other name(s): crocetin GTase; UGTCs2
Systematic name: UDP-glucose:crocetin 8-O-D-glucosyltransferase
Comments: In Crocus sativus this enzyme esterifies a free carboxyl group of crocetin or crocetin glycosyl ester.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Côté, F., Cormier, F., Dufresne, C. and Willemot, C. Properties of a glucosyltransferase involved in crocin synthesis. Plant Sci. 153 (2000) 55-63.
2. Moraga, A.R., Nohales, P.F., Perez, J.A. and Gomez-Gomez, L. Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas. Planta 219 (2004) 955-966. [PMID: 15605174]
Accepted name: soyasapogenol B glucuronide galactosyltransferase
Reaction: UDP-galactose + soyasapogenol B 3-O-β-D-glucuronide = UDP + soyasaponin III
For diagram of reaction click here.
Glossary: soyasaponin III = 3β-(2-O-β-D-galactopyranosyl-β-D-glucopyranosyloxyuronic acid)olean-12-ene-22β,24-diol
Other name(s): UDP-galactose:SBMG-galactosyltransferase; UGT73P2; GmSGT2 (gene name)
Systematic name: UDP-galactose:soyasapogenol B 3-O-glucuronide β-D-galactosyltransferase
Comments: Part of the biosynthetic pathway for soyasaponins.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Shibuya, M., Nishimura, K., Yasuyama, N. and Ebizuka, Y. Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584 (2010) 2258-2264. [PMID: 20350545]
Accepted name: soyasaponin III rhamnosyltransferase
Reaction: UDP-rhamnose + soyasaponin III = UDP + soyasaponin I
For diagram of reaction click here.
Other name(s): UGT91H4; GmSGT3 (gene name)
Systematic name: UDP-rhamnose:soyasaponin III rhamnosyltransferase
Comments: Part of the biosynthetic pathway for soyasaponins.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Shibuya, M., Nishimura, K., Yasuyama, N. and Ebizuka, Y. Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584 (2010) 2258-2264. [PMID: 20350545]
Accepted name: glucosylceramide β-1,4-galactosyltransferase
Reaction: UDP-galactose + β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of reaction click here.
Other name(s): lactosylceramide synthase; uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase; UDP-Gal:glucosylceramide β1→4galactosyltransferase; GalT-2 (misleading)
Systematic name: UDP-galactose:β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase
Comments: Involved in the synthesis of several different major classes of glycosphingolipids.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Chatterjee, S. and Castiglione, E. UDPgalactose:glucosylceramide β1→4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes. Biochim. Biophys. Acta 923 (1987) 136-142. [PMID: 3099851]
2. Trinchera, M., Fiorilli, A. and Ghidoni, R. Localization in the Golgi apparatus of rat liver UDP-Gal:glucosylceramide β1→4galactosyltransferase. Biochemistry 30 (1991) 2719-2724. [PMID: 1900430]
3. Chatterjee, S., Ghosh, N. and Khurana, S. Purification of uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase from human kidney. J. Biol. Chem. 267 (1992) 7148-7153. [PMID: 1551920]
4. Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Wakisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M. and Matsuo, N. Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide β-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273 (1998) 13570-13577. [PMID: 9593693]
5. Takizawa, M., Nomura, T., Wakisaka, E., Yoshizuka, N., Aoki, J., Arai, H., Inoue, K., Hattori, M. and Matsuo, N. cDNA cloning and expression of human lactosylceramide synthase. Biochim. Biophys. Acta 1438 (1999) 301-304. [PMID: 10320813]
Accepted name: lactotriaosylceramide β-1,4-galactosyltransferase
Reaction: UDP-galactose + N-acetyl-β-D-galactosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-galactosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of reaction click here.
Glossary: lactotriaosylceramide = N-acetyl-β-D-galactosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): 4Gal-T4
Systematic name: UDP-galactose:N-acetyl-β-D-galactosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331-29340. [PMID: 9792633]
Accepted name: zeaxanthin glucosyltransferase
Reaction: 2 UDP-glucose + zeaxanthin = 2 UDP + zeaxanthin bis(β-D-glucoside)
For diagram of reaction, click here
Other name(s): crtX (gene name)
Systematic name: UDP-glucose:zeaxanthin β-D-glucosyltransferase
Comments: The reaction proceeds in two steps with the monoglucoside as an intermediate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Hundle, B.S., O'Brien, D.A., Alberti, M., Beyer, P. and Hearst, J.E. Functional expression of zeaxanthin glucosyltransferase from Erwinia herbicola and a proposed uridine diphosphate binding site. Proc. Natl. Acad. Sci. USA 89 (1992) 9321-9325. [PMID: 1409639]
Accepted name: glycosyltransferase DesVII
Reaction: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose + 10-deoxymethynolide = dTDP + 10-deoxymethymycin
For diagram of reaction click here.
Glossary: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose = dTDP-D-desosamine
Other name(s): DesVII
Systematic name: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose:10-deoxymethynolide 3-dimethylamino-4,6-dideoxy-α-D-glucosyltransferase
Comments: DesVII is the glycosyltransferase responsible for the attachment of TDP-D-desosamine to macrolactones of varied ring sizes. The enzyme is involved in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin in Streptomyces venezuelae.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Borisova, S.A. and Liu, H.W. Characterization of glycosyltransferase DesVII and its auxiliary partner protein DesVIII in the methymycin/picromycin biosynthetic pathway. Biochemistry 49 (2010) 8071-8084. [PMID: 20695498]
2. Borisova, S.A., Kim, H.J., Pu, X. and Liu, H.W. Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications. Chembiochem. 9 (2008) 1554-1558. [PMID: 18548476]
3. Hong, J.S., Park, S.J., Parajuli, N., Park, S.R., Koh, H.S., Jung, W.S., Choi, C.Y. and Yoon, Y.J. Functional analysis of desVIII homologues involved in glycosylation of macrolide antibiotics by interspecies complementation. Gene 386 (2007) 123-130. [PMID: 17049185]
Accepted name: desosaminyl transferase EryCIII
Reaction: dTDP-3-dimethylamino-4,6-dideoxy-α-D-glucopyranose + 3-α-mycarosylerythronolide B = dTDP + erythromycin D
Glossary: dTDP-3-dimethylamino-4,6-dideoxy-α-D-glucopyranose = dTDP-D-desosamine
erythromycin D =
(3R,4S,5S,6R,7R,9R,11R,12S,13R,14R)-4-(2,6-dideoxy-3-C-methyl-α-L-ribo-hexopyranosyloxy)-14-ethyl-7,12-dihydroxy-6-[3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyloxy]-3,5,7,9,11,13-hexamethyloxacyclotetradecane-2,10-dione
3-O-α-mycarosylerythronolide B =
(3R,4S,5R,6R,7R,9R,11R,12S,13R,14R)-4-(2,6-dideoxy-3-C-methyl-α-L-ribo-hexopyranosyloxy)-14-ethyl-6,7,12-trihydroxy-3,5,7,9,11,13-hexamethyloxacyclotetradecane-2,10-dione
Other name(s): EryCIII
Systematic name: dTDP-3-dimethylamino-4,6-dideoxy-α-D-glucopyranose:3-α-mycarosylerythronolide B 3-dimethylamino-4,6-dideoxy-α-D-glucosyltransferase
Comments: The enzyme is involved in erythromycin biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Yuan, Y., Chung, H.S., Leimkuhler, C., Walsh, C.T., Kahne, D. and Walker, S. In vitro reconstitution of EryCIII activity for the preparation of unnatural macrolides. J. Am. Chem. Soc. 127 (2005) 14128-14129. [PMID: 16218575]
2. Lee, H.Y., Chung, H.S., Hang, C., Khosla, C., Walsh, C.T., Kahne, D. and Walker, S. Reconstitution and characterization of a new desosaminyl transferase, EryCIII, from the erythromycin biosynthetic pathway. J. Am. Chem. Soc. 126 (2004) 9924-9925. [PMID: 15303858]
3. Moncrieffe, M.C., Fernandez, M.J., Spiteller, D., Matsumura, H., Gay, N.J., Luisi, B.F. and Leadlay, P.F. Structure of the glycosyltransferase EryCIII in complex with its activating P450 homologue EryCII. J. Mol. Biol. 415 (2012) 92-101. [PMID: 22056329]