ExplorEnz: EC 2.4.1.31*

Your query returned 11 entries. Printable version

2.4.1.31

Accepted name:

laminaribiose phosphorylase

Reaction:

3-β-D-glucosyl-D-glucose + phosphate = D-glucose + α-D-glucose 1-phosphate

Systematic name:

3-β-D-glucosyl-D-glucose:phosphate α-D-glucosyltransferase

Comments:

Also acts on 1,3-β-D-oligoglucans. Differs in specificity from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase).

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-29-7

References:

1.	Goldemberg, S.H., Maréchal, L.R. and De Souza, B.C. β-1,3-Oligoglucan: orthophosphate glucosyltransferase from Euglena gracilis. J. Biol. Chem. 241 (1966) 45–50. [PMID: 5901055]
2.	Manners, D.J. and Taylor, D.C. Studies on carbohydrate metabolizing enzymes. XVI. Specificity of laminaribiose phosphorylase from Astasia ocellata. Arch. Biochem. Biophys. 121 (1967) 443–451. [DOI] [PMID: 6057111]

[EC 2.4.1.31 created 1972]

2.4.1.310

Accepted name:

vancomycin aglycone glucosyltransferase

Reaction:

UDP-α-D-glucose + vancomycin aglycone = UDP + devancosaminyl-vancomycin

For diagram of chloroorienticin biosynthesis, click here

Glossary:

devancosaminyl-vancomycin = vancomycin pseudoaglycone

Other name(s):

GtfB (ambiguous)

Systematic name:

UDP-α-D-glucose:vancomycin aglycone 48-O-β-glucosyltransferase

Comments:

The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Losey, H.C., Peczuh, M.W., Chen, Z., Eggert, U.S., Dong, S.D., Pelczer, I., Kahne, D. and Walsh, C.T. Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides. Biochemistry 40 (2001) 4745–4755. [DOI] [PMID: 11294642]
2.	Mulichak, A.M., Losey, H.C., Walsh, C.T. and Garavito, R.M. Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics. Structure 9 (2001) 547–557. [DOI] [PMID: 11470430]

[EC 2.4.1.310 created 2013]

2.4.1.311

Accepted name:

chloroorienticin B synthase

Reaction:

dTDP-β-L-4-epi-vancosamine + desvancosaminyl-vancomycin = dTDP + chloroorienticin B

For diagram of chloroorienticin biosynthesis, click here

Glossary:

dTDP-β-L-4-epi-vancosamine = dTDP-3-amino-2,3,6-trideoxy-3-methyl-β-L-arabino-hexopyranose
desvancosaminyl-vancomycin = vanomycin pseudoaglycone

Other name(s):

GtfA

Systematic name:

dTDP-L-4-epi-vancosamine:desvancosaminyl-vancomycin vancosaminyltransferase

Comments:

The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Mulichak, A.M., Losey, H.C., Lu, W., Wawrzak, Z., Walsh, C.T. and Garavito, R.M. Structure of the TDP-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway. Proc. Natl. Acad. Sci. USA 100 (2003) 9238–9243. [DOI] [PMID: 12874381]
2.	Lu, W., Oberthur, M., Leimkuhler, C., Tao, J., Kahne, D. and Walsh, C.T. Characterization of a regiospecific epivancosaminyl transferase GtfA and enzymatic reconstitution of the antibiotic chloroeremomycin. Proc. Natl. Acad. Sci. USA 101 (2004) 4390–4395. [DOI] [PMID: 15070728]

[EC 2.4.1.311 created 2013]

2.4.1.312

Accepted name:

protein O-mannose β-1,4-N-acetylglucosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + 3-O-(α-D-mannosyl)-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]

For diagram of glycoprotein biosynthesis, click here

Other name(s):

GTDC2 (gene name); POMGNT2

Systematic name:

UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-threonyl-[protein] 4-β-N-acetyl-D-glucosaminyltransferase

Comments:

The human protein is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]

[EC 2.4.1.312 created 2013]

2.4.1.313

Accepted name:

protein O-mannose β-1,3-N-acetylgalactosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-galactosamine + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]

For diagram of glycoprotein biosynthesis, click here

Other name(s):

B3GALNT2

Systematic name:

UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl-threonyl-[protein] 3-β-N-acetyl-D-galactosaminyltransferase

Comments:

The human protein is specific for UDP-N-acetyl-α-D-galactosamine as donor [1]. The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Hiruma, T., Togayachi, A., Okamura, K., Sato, T., Kikuchi, N., Kwon, Y.D., Nakamura, A., Fujimura, K., Gotoh, M., Tachibana, K., Ishizuka, Y., Noce, T., Nakanishi, H. and Narimatsu, H. A novel human β1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcβ1-3GlcNAc. J. Biol. Chem. 279 (2004) 14087–14095. [DOI] [PMID: 14724282]
2.	Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]

[EC 2.4.1.313 created 2013]

2.4.1.314

Accepted name:

ginsenoside Rd glucosyltransferase

Reaction:

UDP-α-D-glucose + ginsenoside Rd = UDP + ginsenoside Rb1

For diagram of protopanaxadiol ginsenosides ginsenosidases, click here

Glossary:

ginsenoside Rd = 20-(β-D-glucopyranosyl)oxy-3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol
ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol

Other name(s):

UDPG:ginsenoside Rd glucosyltransferase; UDP-glucose:ginsenoside Rd glucosyltransferase; UGRdGT

Systematic name:

UDP-glucose:ginsenoside-Rd β-1,6-glucosyltransferase

Comments:

The glucosyl group forms a 1→6 bond to the glucosyloxy moiety at C-20 of ginsenoside Rd. Isolated from sanchi ginseng (Panax notoginseng).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Yue, C.-J. and Zhong J.-J. Purification and characterization of UDPG:ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng. Process Biochem. 40 (2005) 3742–3748.

[EC 2.4.1.314 created 2013]

2.4.1.315

Accepted name:

diglucosyl diacylglycerol synthase (1,6-linking)

Reaction:

(1) UDP-α-D-glucose + 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP
(2) UDP-α-D-glucose + 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP

Other name(s):

monoglucosyl diacylglycerol (1→6) glucosyltransferase; MGlcDAG (1→6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name)

Systematic name:

UDP-α-D-glucose:1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol 6-glucosyltransferase

Comments:

The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose [1]. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo [3]. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1′-sn-glycerol) [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Jorasch, P., Wolter, F.P., Zahringer, U. and Heinz, E. A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. Mol. Microbiol. 29 (1998) 419–430. [DOI] [PMID: 9720862]
2.	Jorasch, P., Warnecke, D.C., Lindner, B., Zahringer, U. and Heinz, E. Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols. Eur. J. Biochem. 267 (2000) 3770–3783. [DOI] [PMID: 10848996]
3.	Andres, E., Martinez, N. and Planas, A. Expression and characterization of a Mycoplasma genitalium glycosyltransferase in membrane glycolipid biosynthesis: potential target against mycoplasma infections. J. Biol. Chem. 286 (2011) 35367–35379. [DOI] [PMID: 21835921]

[EC 2.4.1.315 created 2014]

2.4.1.316

Accepted name:

tylactone mycaminosyltransferase

Reaction:

tylactone + dTDP-α-D-mycaminose = dTDP + 5-O-β-D-mycaminosyltylactone

For diagram of tylactone biosynthesis, click here

Glossary:

tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyloxacyclohexadeca-11,13-diene-2,10-dione
dTDP-α-D-mycaminose = dTDP-3,6-dideoxy-3-dimethylamino-α-D-glucopyranose

Other name(s):

tylM2 (gene name)

Systematic name:

dTDP-α-D-mycaminose:tylactone 5-O-β-D-mycaminosyltransferase

Comments:

The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. Activity is significantly enhanced by the presence of an accessory protein encoded by the tylM3 gene.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Gandecha, A.R., Large, S.L. and Cundliffe, E. Analysis of four tylosin biosynthetic genes from the tylLM region of the Streptomyces fradiae genome. Gene 184 (1997) 197–203. [DOI] [PMID: 9031628]
2.	Melancon, C.E., 3rd, Takahashi, H. and Liu, H.W. Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient glycosyltransfer in macrolide antibiotic biosynthesis. J. Am. Chem. Soc. 126 (2004) 16726–16727. [DOI] [PMID: 15612702]

[EC 2.4.1.316 created 2014]

2.4.1.317

Accepted name:

O-mycaminosyltylonolide 6-deoxyallosyltransferase

Reaction:

5-O-β-D-mycaminosyltylonolide + dTDP-6-deoxy-α-D-allose = dTDP + demethyllactenocin

For diagram of tylosin biosynthesis, click here

Glossary:

mycaminose = 3,6-dideoxy-3-dimethylamino-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxooxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-β-D-allopyranoside

Other name(s):

tylN (gene name)

Systematic name:

dTDP-6-deoxy-α-D-allose:5-O-β-D-mycaminosyltylonolide 23-O-6-deoxy-α-D-allosyltransferase

Comments:

The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Wilson, V.T. and Cundliffe, E. Characterization and targeted disruption of a glycosyltransferase gene in the tylosin producer, Streptomyces fradiae. Gene 214 (1998) 95–100. [DOI] [PMID: 9651492]

[EC 2.4.1.317 created 2014]

2.4.1.318

Accepted name:

demethyllactenocin mycarosyltransferase

Reaction:

dTDP-β-L-mycarose + demethyllactenocin = dTDP + demethylmacrocin

For diagram of tylosin biosynthesis, click here

Glossary:

dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-D-allopyranoside

Other name(s):

tylCV (gene name); tylC5 (gene name)

Systematic name:

dTDP-β-L-mycarose:demethyllactenocin 4′-O-α-L-mycarosyltransferase

Comments:

The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Bate, N., Butler, A.R., Smith, I.P. and Cundliffe, E. The mycarose-biosynthetic genes of Streptomyces fradiae, producer of tylosin. Microbiology 146 (2000) 139–146. [DOI] [PMID: 10658660]

[EC 2.4.1.318 created 2014]

2.4.1.319

Accepted name:

β-1,4-mannooligosaccharide phosphorylase

Reaction:

[(1→4)-β-D-mannosyl]_n + phosphate = [(1→4)-β-D-mannosyl]_n-1 + α-D-mannose 1-phosphate

Other name(s):

RaMP2

Systematic name:

1,4-β-D-mannooligosaccharide:phosphate α-D-mannosyltransferase

Comments:

The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyses the reversible phosphorolysis of β-1,4-mannooligosaccharide with a minimum size of three monomers.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

Kawahara, R., Saburi, W., Odaka, R., Taguchi, H., Ito, S., Mori, H. and Matsui, H. Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus, involving two mannoside phosphorylases and cellobiose 2-epimerase: discovery of a new carbohydrate phosphorylase, β-1,4-mannooligosaccharide phosphorylase. J. Biol. Chem. 287 (2012) 42389–42399. [DOI] [PMID: 23093406]

[EC 2.4.1.319 created 2014]