The Enzyme Database

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EC 2.4.1.243     Relevance: 100%
Accepted name: 6G-fructosyltransferase
Reaction: [1-β-D-fructofuranosyl-(2→1)-]m+1-α-D-glucopyranoside + [1-β-D-fructofuranosyl-(2→1)-]n-α-D-glucopyranoside = [1-β-D-fructofuranosyl-(2→1)-]m-α-D-glucopyranoside + [1-β-D-fructofuranosyl-(2→1)-]n-β-D-fructofuranosyl-(2→6)-α-D-glucopyranoside (m > 0; n ≥ 0)
Glossary: [1-β-D-fructofuranosyl-(2→1)-]n-α-D-glucopyranoside = inulin
Other name(s): fructan:fructan 6G-fructosyltransferase; 1F(1-β-D-fructofuranosyl)m sucrose:1F(1-β-D-fructofuranosyl)nsucrose 6G-fructosyltransferase; 6G-FFT; 6G-FT; 6G-fructotransferase
Systematic name: 1F-oligo[β-D-fructofuranosyl-(2→1)-]sucrose 6G-β-D-fructotransferase
Comments: Inulins are polysaccharides consisting of linear or branched D-fructofuranosyl chains attached to the fructosyl residue of sucrose by a β(2→1) linkage. This enzyme catalyses the transfer of the terminal (2→1)-linked -D-fructosyl group of an inulin chain onto O-6 position of the glucose residue of another inulin molecule [1]. For example, if 1-kestose [1F-(β-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6G-di-β-D-fructofuranosylsucrose. In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent. Alternatively, this may be indicated by the presence and/or absence of primes (see http://www.chem.qmul.ac.uk/iupac/2carb/36.html#362). Sucrose cannot be a donor substrate in the reaction (i.e. m cannot be zero) and inulin cannot act as an acceptor. Side reactions catalysed are transfer of a β-D-fructosyl group between compounds of the structure 1F-(1-β-D-fructofuranosyl)m-6G-(1-β-D-fructofuranosyl)n sucrose, where m ≥ 0 and n = 1 for the donor, and m ≥ 0 and n ≥ 0 for the acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79633-28-6
References:
1.  Shiomi, N. Purification and characterisation of 6G-fructosyltransferase from the roots of asparagus (Asparagus officinalis L.). Carbohydr. Res. 96 (1981) 281–292.
2.  Shiomi, N. Reverse reaction of fructosyl transfer catalysed by asparagus 6G-fructosyltransferase. Carbohydr. Res. 106 (1982) 166–169.
3.  Shiomi, N. and Ueno, K. Cloning and expression of genes encoding fructosyltransferases from higher plants in food technology. J. Appl. Glycosci. 51 (2004) 177–183.
4.  Ueno, K., Onodera, S., Kawakami, A., Yoshida, M. and Shiomi, N. Molecular characterization and expression of a cDNA encoding fructan:fructan 6G-fructosyltransferase from asparagus (Asparagus officinalis). New Phytol. 165 (2005) 813–824. [DOI] [PMID: 15720693]
[EC 2.4.1.243 created 2006]
 
 
EC 3.2.1.154     Relevance: 91.6%
Accepted name: fructan β-(2,6)-fructosidase
Reaction: Hydrolysis of terminal, non-reducing (2→6)-linked β-D-fructofuranose residues in fructans
For diagram of reaction, click here
Other name(s): β-(2-6)-fructan exohydrolase; levanase; 6-FEH; β-(2,6)-D-fructan fructohydrolase
Systematic name: (2→6)-β-D-fructan fructohydrolase
Comments: Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the levan-type fructans such as 6-kestotriose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside] and 6,6-kestotetraose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) inulin-type fructans can also be hydrolysed, but more slowly [cf. EC 3.2.1.153, fructan β-(2,1)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000597-62-5
References:
1.  Marx, S.P., Nösberger, J. and Frehner, M. Hydrolysis of fructan in grasses: A β-(2-6)-linkage specific fructan-β-fructosidase from stubble of Lolium perenne. New Phytol. 135 (1997) 279–290.
2.  Van den Ende, W., De Coninck, B., Clerens, S., Vergauwen, R. and Van Laere, A. Unexpected presence of fructan 6-exohydrolases (6-FEHs) in non-fructan plants: characterization, cloning, mass mapping and functional analysis of a novel 'cell-wall invertase-like' specific 6-FEH from sugar beet (Beta vulgaris L.). Plant J. 36 (2003) 697–710. [DOI] [PMID: 14617070]
3.  Henson, C.A. and Livingston, D.P. , III. Purification and characterization of an oat fructan exohydrolase that preferentially hydrolyzes β-2,6-fructans. Plant Physiol. 110 (1996) 639–644. [PMID: 8742337]
[EC 3.2.1.154 created 2005]
 
 
EC 3.2.1.153     Relevance: 88.9%
Accepted name: fructan β-(2,1)-fructosidase
Reaction: Hydrolysis of terminal, non-reducing (2→1)-linked β-D-fructofuranose residues in fructans
For diagram of reaction, click here
Other name(s): β-(2-1)-D-fructan fructohydrolase; β-(2-1)fructan exohydrolase; inulinase; 1-FEH II; 1-fructan exohydrolase; 1-FEH w1; 1-FEH w2; β-(2-1)-linkage-specific fructan-β-fructosidase; β-(2,1)-D-fructan fructohydrolase
Systematic name: β-(2→1)-D-fructan fructohydrolase
Comments: Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the inulin-type fructans, such as 1-kestose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside] and 1,1-nystose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) levan-type fructans can also be hydrolysed, but more slowly [see EC 3.2.1.154, fructan β-(2,6)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1000593-08-7
References:
1.  De Roover, J., Van Laere, A., De Winter, M., Timmermans, J.W. and Van den Ende, W. Purification and properties of a second fructan exohydrolase from the roots of Cichorium intybus. Physiol. Plant. 106 (1999) 28–34.
2.  Van den Ende, W., Clerens, S., Vergauwen, R., Van Riet, L., Van Laere, A., Yoshida, M. and Kawakami, A. Fructan 1-exohydrolases. β-(2,1)-Trimmers during graminan biosynthesis in stems of wheat? Purification, characterization, mass mapping, and cloning of two fructan 1-exohydrolase isoforms. Plant Physiol. 131 (2003) 621–631. [DOI] [PMID: 12586886]
[EC 3.2.1.153 created 2005]
 
 
EC 2.4.1.10     Relevance: 88.4%
Accepted name: levansucrase
Reaction: sucrose + [6)-β-D-fructofuranosyl-(2→]n α-D-glucopyranoside = D-glucose + [6)-β-D-fructofuranosyl-(2→]n+1 α-D-glucopyranoside
For diagram of reaction, click here
Other name(s): sucrose 6-fructosyltransferase; β-2,6-fructosyltransferase; β-2,6-fructan:D-glucose 1-fructosyltransferase; sucrose:2,6-β-D-fructan 6-β-D-fructosyltransferase; sucrose:(2→6)-β-D-fructan 6-β-D-fructosyltransferase
Systematic name: sucrose:[6)-β-D-fructofuranosyl-(2→]n α-D-glucopyranoside 6-β-D-fructosyltransferase
Comments: Some other sugars can act as D-fructosyl acceptors.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-17-5
References:
1.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337. [PMID: 24540594]
2.  Hestrin, S., Feingold, D.S. and Avigad, G. The mechanism of polysaccharide production from sucrose. 3. Donor-acceptor specificity of levansucrase from Aerobacter levanicum. Biochem. J. 64 (1956) 340–351. [PMID: 13363847]
3.  Reese, E.T. and Avigad, G. Purification of levansucrase by precipitation with levan. Biochim. Biophys. Acta 113 (1966) 79–83. [PMID: 5940635]
4.  Meng, G. and Futterer, K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nat. Struct. Biol. 10 (2003) 935–941. [DOI] [PMID: 14517548]
[EC 2.4.1.10 created 1961, modified 2011]
 
 
EC 2.4.1.99     Relevance: 67.3%
Accepted name: sucrose:sucrose fructosyltransferase
Reaction: 2 sucrose = D-glucose + β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside
Other name(s): SST; sucrose:sucrose 1-fructosyltransferase; sucrose-sucrose 1-fructosyltransferase; sucrose 1F-fructosyltransferase; sucrose:sucrose 1F-β-D-fructosyltransferase
Systematic name: sucrose:sucrose 1′-β-D-fructosyltransferase
Comments: For definition of the prime in the systematic name, see 2-Carb-36.2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73379-56-3
References:
1.  Henry, R.J. and Darbyshire, B. Sucrose:sucrose fructosyltransferase and fructan:fructan fructosyltransferase from Allium cepa. Phytochemistry 19 (1980) 1017–1020.
2.  Lüscher, M., Hochstrasser, U., Vogel, G., Aeschbacher, R., Galati, V., Nelson, C.J., Boller, T. and Wiemken, A. Cloning and functional analysis of sucrose:sucrose 1-fructosyltransferase from tall fescue. Plant Physiol. 124 (2000) 1217–1228. [PMID: 11080298]
[EC 2.4.1.99 created 1981, modified 2004]
 
 
EC 3.1.3.79     Relevance: 61.3%
Accepted name: mannosylfructose-phosphate phosphatase
Reaction: β-D-fructofuranosyl-α-D-mannopyranoside 6F-phosphate + H2O = β-D-fructofuranosyl-α-D-mannopyranoside + phosphate
Glossary: mannosylfructose = β-D-fructofuranosyl-α-D-mannopyranoside
Other name(s): mannosylfructose-6-phosphate phosphatase; MFPP
Systematic name: β-D-fructofuranosyl-α-D-mannopyranoside-6F-phosphate phosphohydrolase
Comments: This enzyme, from the soil proteobacterium and plant pathogen Agrobacterium tumefaciens strain C58, requires Mg2+ for activity. Mannosylfructose is the major endogenous osmolyte produced by several α-proteobacteria in response to osmotic stress and is synthesized by the sequential action of EC 2.4.1.246 (mannosylfructose-phosphate synthase) followed by this enzyme. While mannosylfructose 6-phosphate is the physiological substrate, the enzyme can use sucrose 6-phosphate very efficiently. The F in mannosylfructose 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Torres, L.L. and Salerno, G.L. A metabolic pathway leading to mannosylfructose biosynthesis in Agrobacterium tumefaciens uncovers a family of mannosyltransferases. Proc. Natl. Acad. Sci. USA 104 (2007) 14318–14323. [DOI] [PMID: 17728402]
[EC 3.1.3.79 created 2009]
 
 
EC 2.4.1.166     Relevance: 56.1%
Accepted name: raffinose—raffinose α-galactosyltransferase
Reaction: 2 raffinose = 1F-α-D-galactosylraffinose + sucrose
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): raffinose (raffinose donor) galactosyltransferase; raffinose:raffinose α-galactosyltransferase; raffinose—raffinose α-galactotransferase
Systematic name: raffinose:raffinose α-D-galactosyltransferase
Comments: The 3F position of raffinose can also act as galactosyl acceptor; the enzyme is involved in the accumulation of the tetrasaccharides lychnose and isolychnose in the leaves of Cerastium arvense and other plants of the family Caryophyllaceae during late autumn.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93389-38-9
References:
1.  Hopf, H., Gruber, G., Zinn, A. and Kandler, O. Physiology and biosynthesis of lychnose in Cerastium arvense. Planta 162 (1984) 283–288. [PMID: 24253101]
[EC 2.4.1.166 created 1989]
 
 
EC 3.2.1.149     Relevance: 53.5%
Accepted name: β-primeverosidase
Reaction: a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside + H2O = 6-O-(β-D-xylopyranosyl)-β-D-glucopyranose + an alcohol
Glossary: primeverose = 6-O-(β-D-xylopyranosyl)-D-glucose
vicianose = 6-O-(α-L-arabinopyranosyl)-D-glucose
Systematic name: 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside 6-O-(β-D-xylosyl)-β-D-glucohydrolase
Comments: The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. In addition to β-primeverosides [i.e. 6-O-(β-D-xylopyranosyl)-β-D-glucopyranosides], it also hydrolyses 6-O-(β-D-apiofuranosyl)-β-D-glucopyranosides and, less rapidly, β-vicianosides and 6-O-(α-L-arabinofuranosyl)-β-D-glucopyranosides, but not β-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 884593-92-4
References:
1.  Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M., Nagata, T. and Sakata, K. Characterization of β-primeverosidase, being concerned with alcoholic aroma formation in tea leaves to be processed into black tea, and preliminary observations on its substrate specificity. J. Agric. Food Chem. 46 (1998) 1712–1718.
2.  Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S., Tong, Q. and Sakata, K. Purification of a β-primeverosidase concerned with alcoholic aroma formation in tea leaves (cv. Shuxian) to be processed to oolong tea. J. Agric. Food Chem. 45 (1997) 877–882.
[EC 3.2.1.149 created 2001]
 
 
EC 3.2.1.168     Relevance: 51.6%
Accepted name: hesperidin 6-O-α-L-rhamnosyl-β-D-glucosidase
Reaction: hesperidin + H2O = hesperetin + rutinose
Glossary: hesperetin = 5,7,3′-trihydroxy-4′-methoxyflavanone
hesperidin = hesperetin 7-(6-O-α-L-rhamnopyranosyl-β-D-glucopyranoside)
rutinose = 6-O-α-L-rhamnopyranosyl-D-glucose
Other name(s): AnRut; rutinosidase
Systematic name: hesperetin 7-(6-O-α-L-rhamnopyranosyl-β-D-glucopyranoside) 6-O-α-rhamnopyranosyl-β-glucohydrolase
Comments: The enzyme exhibits high specificity towards 7-O-linked flavonoid β-rutinosides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mazzaferro, L., Piñuel, L., Minig, M. and Breccia, J.D. Extracellular monoenzyme deglycosylation system of 7-O-linked flavonoid β-rutinosides and its disaccharide transglycosylation activity from Stilbella fimetaria. Arch. Microbiol. 192 (2010) 383–393. [DOI] [PMID: 20358178]
2.  Mazzaferro, L., Piñuel, L., Minig, M. and Breccia, J.D. Erratum to: Extracellular monoenzyme deglycosylation system of 7-O-linked flavonoid β-rutinosides and its disaccharide transglycosylation activity from Stilbella fimetaria. Arch. Microbiol. 193 (2011) 461.
[EC 3.2.1.168 created 2011]
 
 
EC 2.4.1.82     Relevance: 51.3%
Accepted name: galactinol—sucrose galactosyltransferase
Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + sucrose = myo-inositol + raffinose
For diagram of stachyose biosynthesis, click here
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): 1-α-D-galactosyl-myo-inositol:sucrose 6-α-D-galactosyltransferase; α-D-galactosyl-(1→3)-myo-inositol:sucrose 6-α-D-galactosyltransferase; raffinose synthase; RafS
Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:sucrose 6-α-D-galactosyltransferase
Comments: 4-Nitrophenyl α-D-galactopyranoside can also act as donor. The enzyme also catalyses an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123, inositol 3-α-galactosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-45-0
References:
1.  Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [DOI] [PMID: 4774118]
2.  Lehle, L., Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of raffinose. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 1494–1498. [PMID: 5491608]
[EC 2.4.1.82 created 1976, modified 2003]
 
 
EC 3.2.1.190     Relevance: 49.8%
Accepted name: dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming)
Reaction: 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin + 2 H2O = 2 L-rhamnopyranose + diosgenin 3-O-β-D-glucopyranoside
For diagram of diosgenin catabolism, click here
Glossary: 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin = (3β,25R)-spirost-5-en-3-yl 6-deoxy-α-L-mannopyranosyl-(1→2)-[6-deoxy-α-L-mannopyranosyl-(1→4)]-β-D-glucopyranoside = dioscin
diosgenin = (3β,25R)-spirost-5-en-3-ol
Other name(s): dioscin-α-L-rhamnosidase
Systematic name: 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin (3-O-β-D-Glc-diosgenin-forming)
Comments: The enzyme is involved in the hydrolysis of the steroid saponin dioscin by the digestive system of Sus scrofa (pig). cf. EC 3.2.1.189, dioscin glycosidase (diosgenin-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Qian, S., Yu, H., Zhang, C., Lu, M., Wang, H. and Jin, F. Purification and characterization of dioscin-α-L-rhamnosidase from pig liver. Chem Pharm Bull (Tokyo) 53 (2005) 911–914. [PMID: 16079518]
[EC 3.2.1.190 created 2013]
 
 
EC 1.14.20.2      
Transferred entry: 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase. Now EC 1.14.11.59, 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase
[EC 1.14.20.2 created 2012, deleted 2018]
 
 
EC 1.14.11.59     Relevance: 49.2%
Accepted name: 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase
Reaction: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + 2-oxoglutarate + O2 = (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + succinate + CO2 + H2O
For diagram of benzoxazinone biosynthesis, click here
Glossary: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIBOA β-D-glucoside
(2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = TRIBOA β-D-glucoside
Other name(s): BX6 (gene name); DIBOA-Glc dioxygenase
Systematic name: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside:oxygen oxidoreductase (7-hydroxylating)
Comments: The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jonczyk, R., Schmidt, H., Osterrieder, A., Fiesselmann, A., Schullehner, K., Haslbeck, M., Sicker, D., Hofmann, D., Yalpani, N., Simmons, C., Frey, M. and Gierl, A. Elucidation of the final reactions of DIMBOA-glucoside biosynthesis in maize: characterization of Bx6 and Bx7. Plant Physiol. 146 (2008) 1053–1063. [DOI] [PMID: 18192444]
[EC 1.14.11.59 created 2012 as EC 1.14.20.2, transferred 2018 to EC 1.14.11.59]
 
 
EC 2.4.1.67     Relevance: 48.3%
Accepted name: galactinol—raffinose galactosyltransferase
Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + raffinose = myo-inositol + stachyose
For diagram of stachyose biosynthesis, click here
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): galactinol-raffinose galactosyltransferase; stachyose synthetase; α-D-galactosyl-(1→3)-myo-inositol:raffinose galactosyltransferase
Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:raffinose galactosyltransferase
Comments: This enzyme also catalyses galactosyl transfer from stachyose to raffinose (shown by labelling) [4]. For synthesis of the substrate, see EC 2.4.1.123, inositol 3-α-galactosyltransferase. See also EC 2.4.1.82, galactinol—sucrose galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-70-6
References:
1.  Tanner, W. Die Biosynthese der Stachyose. Ber. Dtsch. Bot. Ges. 80 (1967) 111.
2.  Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of stachyose. Eur. J. Biochem. 4 (1968) 233–239. [DOI] [PMID: 5655499]
3.  Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [DOI] [PMID: 4774118]
4.  Kandler, O. and Hopf, H. Occurrence, metabolism and function of oligosaccharides. In: Preiss, J. (Ed.), The Biochemistry of Plant, vol. 3, Academic Press, New York, 1980, pp. 221–270.
[EC 2.4.1.67 created 1972, modified 2003]
 
 
EC 2.1.1.241     Relevance: 46.4%
Accepted name: 2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase
Reaction: S-adenosyl-L-methionine + (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = S-adenosyl-L-homocysteine + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
For diagram of benzoxazinone biosynthesis, click here
Glossary: (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = TRIMBOA β-D-glucoside
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIMBOA β-D-glucoside
Other name(s): BX7 (gene name); OMT BX7
Systematic name: S-adenosyl-L-methionine:(2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside 7-O-methyltransferase
Comments: The enzyme is involved in the biosynthesis of the protective and allelophatic benzoxazinoid DIMBOA [(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin] in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jonczyk, R., Schmidt, H., Osterrieder, A., Fiesselmann, A., Schullehner, K., Haslbeck, M., Sicker, D., Hofmann, D., Yalpani, N., Simmons, C., Frey, M. and Gierl, A. Elucidation of the final reactions of DIMBOA-glucoside biosynthesis in maize: characterization of Bx6 and Bx7. Plant Physiol. 146 (2008) 1053–1063. [DOI] [PMID: 18192444]
[EC 2.1.1.241 created 2012]
 
 
EC 2.4.1.202     Relevance: 46.3%
Accepted name: 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = UDP + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
(2) UDP-α-D-glucose + 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = UDP + (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
For diagram of benzoxazinone biosynthesis, click here
Glossary: 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = DIBOA
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = DIMBOA
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIBOA β-D-glucoside
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIMBOA β-D-glucoside
Other name(s): uridine diphosphoglucose-2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-glucosyltransferase; BX8; BX9; benzoxazinoid glucosyltransferase; DIMBOA glucosyltransferase
Systematic name: UDP-α-D-glucose:2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-β-D-glucosyltransferase
Comments: The enzyme is involved in the detoxification of the benzoxazinoids DIBOA (2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one) and DIMBOA (2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one) which are stored as the respective non-toxic glucosides in the vacuoles in some plants, most commonly from the family of Poaceae (grasses). Benzoxazinoids are known to exhibit antimicrobial, antifeedant, and antiinsecticidal effects and are involved in the interaction of plants with other plants, insects, or microorganisms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122544-56-3
References:
1.  Bailey, B.A. and Larson, R.L. Hydroxamic acid glucosyltransferases from maize seedlings. Plant Physiol. 90 (1989) 1071–1076. [PMID: 16666853]
2.  von Rad, U., Huttl, R., Lottspeich, F., Gierl, A. and Frey, M. Two glucosyltransferases are involved in detoxification of benzoxazinoids in maize. Plant J. 28 (2001) 633–642. [DOI] [PMID: 11851909]
[EC 2.4.1.202 created 1992, modified 2012]
 
 
EC 2.4.1.246     Relevance: 45.8%
Accepted name: mannosylfructose-phosphate synthase
Reaction: GDP-mannose + D-fructose 6-phosphate = GDP + β-D-fructofuranosyl-α-D-mannopyranoside 6F-phosphate
Glossary: mannosylfructose = β-D-fructofuranosyl-α-D-mannopyranoside
Other name(s): mannosylfructose-6-phosphate synthase; MFPS
Systematic name: GDP-mannose:D-fructose-6-phosphate 2-α-D-mannosyltransferase
Comments: This enzyme, from the soil proteobacterium and plant pathogen Agrobacterium tumefaciens strain C58, requires Mg2+ or Mn2+ for activity. GDP-mannose can be replaced by ADP-mannose but with a concomitant decrease in activity. The product of this reaction is dephosphorylated by EC 3.1.3.79 (mannosylfructose-phosphate phosphatase) to form the non-reducing disaccharide mannosylfructose, which is the major endogenous osmolyte produced by several α-proteobacteria in response to osmotic stress. The F in the product name is used to indicate that the fructose residue of sucrose carries the substituent.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 92480-04-1 (not distinguished from EC 2.4.1.167)
References:
1.  Torres, L.L. and Salerno, G.L. A metabolic pathway leading to mannosylfructose biosynthesis in Agrobacterium tumefaciens uncovers a family of mannosyltransferases. Proc. Natl. Acad. Sci. USA 104 (2007) 14318–14323. [DOI] [PMID: 17728402]
[EC 2.4.1.246 created 2008]
 
 
EC 3.2.1.161     Relevance: 45.6%
Accepted name: β-apiosyl-β-glucosidase
Reaction: 7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + β-D-apiofuranosyl-(1→6)-D-glucose
Other name(s): isoflavonoid-7-O-β[D-apiosyl-(1→6)-β-D-glucoside] disaccharidase; isoflavonoid 7-O-β-apiosyl-glucoside β-glucosidase; furcatin hydrolase
Systematic name: 7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid β-D-apiofuranosyl-(1→6)-D-glucohydrolase
Comments: The enzyme from the tropical tree Dalbergia nigrescens Kurz belongs in glycosyl hydrolase family 1. The enzyme removes disaccharides from the natural substrates dalpatein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside and 7-hydroxy-2′,4′,5′,6-tetramethoxy-7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside (dalnigrein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides [2]. Daidzin and genistin are also substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000598-83-3
References:
1.  Hosel, W. and Barz, W. β-Glucosidases from Cicer arietinum L. Purification and Properties of isoflavone-7-O-glucoside-specific β-glucosidases. Eur. J. Biochem. 57 (1975) 607–616. [DOI] [PMID: 240725]
2.  Chuankhayan, P., Hua, Y., Svasti, J., Sakdarat, S., Sullivan, P.A. and Ketudat Cairns, J.R. Purification of an isoflavonoid 7-O-β-apiosyl-glucoside β-glycosidase and its substrates from Dalbergia nigrescens Kurz. Phytochemistry 66 (2005) 1880–1889. [DOI] [PMID: 16098548]
3.  Ahn, Y.O., Mizutani, M., Saino, H. and Sakata, K. Furcatin hydrolase from Viburnum furcatum Blume is a novel disaccharide-specific acuminosidase in glycosyl hydrolase family 1. J. Biol. Chem. 279 (2004) 23405–23414. [DOI] [PMID: 14976214]
[EC 3.2.1.161 created 2006]
 
 
EC 2.4.1.301     Relevance: 45.1%
Accepted name: 2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase
Reaction: (1) UDP-α-D-kanosamine + 2′-deamino-2′-hydroxyneamine = UDP + kanamycin A
(2) UDP-α-D-kanosamine + neamine = UDP + kanamycin B
(3) UDP-α-D-kanosamine + paromamine = UDP + kanamycin C
(4) UDP-α-D-kanosamine + 2′-deamino-2′-hydroxyparomamine = UDP + kanamycin X
For diagram of kanamycin A biosynthesis, click here
Glossary: neamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
paromamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
UDP-α-D-kanosamine = uridine 5′-[3-(3-amino-3-deoxy-α-D-glucopyranosyl) diphosphate]
kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
kanamycin B = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
kanamycin C = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
kanamycin X = (1S,2R,3R,4S,6R)-4,6-diamino-3-(α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
Other name(s): kanE (gene name); kanM2 (gene name)
Systematic name: UDP-α-D-kanosamine:2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase
Comments: Involved in the biosynthetic pathway of kanamycins. The enzyme characterized from the bacterium Streptomyces kanamyceticus can also accept UDP-α-D-glucose with lower efficiency [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kudo, F., Sucipto, H. and Eguchi, T. Enzymatic activity of a glycosyltransferase KanM2 encoded in the kanamycin biosynthetic gene cluster. J. Antibiot. (Tokyo) 62 (2009) 707–710. [DOI] [PMID: 19911031]
2.  Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602]
[EC 2.4.1.301 created 2013]
 
 
EC 3.2.1.182     Relevance: 44.4%
Accepted name: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside β-D-glucosidase
Reaction: (1) (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + H2O = 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose
(2) (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + H2O = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose
Glossary: DIMBOA glucoside = (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
DIBOA glucoside = (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
Other name(s): DIMBOAGlc hydrolase; DIMBOA glucosidase
Systematic name: (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside β-D-glucosidase
Comments: The enzyme from Triticum aestivum (wheat) has a higher affinity for DIMBOA glucoside than DIBOA glucoside. With Secale cereale (rye) the preference is reversed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sue, M., Ishihara, A. and Iwamura, H. Purification and characterization of a hydroxamic acid glucoside β-glucosidase from wheat (Triticum aestivum L.) seedlings. Planta 210 (2000) 432–438. [PMID: 10750901]
2.  Sue, M., Ishihara, A. and Iwamura, H. Purification and characterization of a β-glucosidase from rye (Secale cereale L.) seedlings. Plant Sci. 155 (2000) 67–74. [DOI] [PMID: 10773341]
3.  Czjzek, M., Cicek, M., Zamboni, V., Bevan, D.R., Henrissat, B. and Esen, A. The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes. Proc. Natl. Acad. Sci. USA 97 (2000) 13555–13560. [DOI] [PMID: 11106394]
4.  Nikus, J., Esen, A. and Jonsson, L.M.V. Cloning of a plastidic rye (Secale cereale) β-glucosidase cDNA and its expression in Escherichia coli. Physiol. Plantarum 118 (2003) 337–348.
5.  Sue, M., Yamazaki, K., Yajima, S., Nomura, T., Matsukawa, T., Iwamura, H. and Miyamoto, T. Molecular and structural characterization of hexameric β-D-glucosidases in wheat and rye. Plant Physiol. 141 (2006) 1237–1247. [DOI] [PMID: 16751439]
6.  Sue, M., Nakamura, C., Miyamoto, T. and Yajima, S. Active-site architecture of benzoxazinone-glucoside β-D-glucosidases in Triticeae. Plant Sci. 180 (2011) 268–275. [DOI] [PMID: 21421370]
[EC 3.2.1.182 created 2012]
 
 
EC 2.4.1.365     Relevance: 42.2%
Accepted name: protopanaxadiol-type ginsenoside-3-O-glucoside 2′′-O-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + (20S)-ginsenoside Rh2 = UDP + (20S)-ginsenoside Rg3
(2) UDP-α-D-glucose + ginsenoside F2 = UDP + ginsenoside Rd
Glossary: (20S)-ginsenoside Rh2 = (3β,12β)-12,20-dihydroxydammar-24-en-3-yl β-D-glucopyranoside
ginsenoside F2 = (3β,12β)-20-(β-D-glucopyranosyloxy)-12-hydroxydammar-24-en-3-yl β-D-glucopyranoside
Other name(s): UGT94Q2 (gene name)
Systematic name: UDP-α-D-glucose:3-O-glucosyl-protopanaxadiol-type ginsenoside 2′′-O-glucosyltransferase
Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the 2′′ position of the glucose moiety in the protopanaxadiol-type ginsenoside-3-O-glucosides (20S)-ginsenoside Rh2 and ginsenoside F2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jung, S.C., Kim, W., Park, S.C., Jeong, J., Park, M.K., Lim, S., Lee, Y., Im, W.T., Lee, J.H., Choi, G. and Kim, S.C. Two ginseng UDP-glycosyltransferases synthesize ginsenoside Rg3 and Rd. Plant Cell Physiol. 55 (2014) 2177–2188. [PMID: 25320211]
[EC 2.4.1.365 created 2019]
 
 
EC 3.2.1.189     Relevance: 39.9%
Accepted name: dioscin glycosidase (diosgenin-forming)
Reaction: 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin + 3 H2O = D-glucose + 2 L-rhamnose + diosgenin
For diagram of diosgenin catabolism, click here
Glossary: 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin = (3β,25R)-spirost-5-en-3-yl 6-deoxy-α-L-mannopyranosyl-(1→2)-[6-deoxy-α-L-mannopyranosyl-(1→4)]-β-D-glucopyranoside = dioscin
diosgenin = (3β,25R)-spirost-5-en-3-ol
Other name(s): dioscin glycosidase (aglycone-forming)
Systematic name: 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin hydrolase (diosgenin-forming)
Comments: The enzyme is involved in degradation of the steroid saponin dioscin by some fungi of the Absidia genus. The enzyme can also hydrolyse 3-O-[α-L-Ara-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin into diosgenin and free sugars as the final products. cf. EC 3.2.1.190, dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fu, Y., Yu, H., Tang, S.H., Hu, X., Wang, Y., Liu, B., Yu, C. and Jin, F. New dioscin-glycosidase hydrolyzing multi-glycosides of dioscin from Absidia strain. J. Microbiol. Biotechnol. 20 (2010) 1011–1017. [PMID: 20622501]
[EC 3.2.1.189 created 2013]
 
 
EC 2.1.3.14      
Deleted entry: tobramycin carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5′ synthase
[EC 2.1.3.14 created 2013, deleted 2014]
 
 
EC 4.2.1.178     Relevance: 37.5%
Accepted name: difructose-dianhydride-III synthase
Reaction: inulobiose = α-D-fructofuranose-β-D-fructofuranose 2′,1:2,3′-dianhydride + H2O
Glossary: difructose anhydride III = α-D-fructofuranose-β-D-fructofuranose 2′,1:2,3′-dianhydride
inulobiose = β-D-fructofuranosyl-(2→1)-D-fructose
Other name(s): DFA-IIIase; difructose anhydride III hydrolase
Systematic name: inulobiose hydro-lyase (α-D-fructofuranose-β-D-fructofuranose 2′,1:2,3′-dianhydride-forming)
Comments: The enzyme participates in an inulin degradation pathway, in which it forms inulobiose from difructose anhydride III. A conformational change in the enzyme from the bacterium Pseudarthrobacter chlorophenolicus results in it also catalysing the activity of EC 4.2.2.18, inulin fructotransferase (DFA-III-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tanaka, T., Uchiyama, T., Kobori, H. and Tanaka, K. Enzymic hydrolysis of di-D-fructofuranose 1, 2′; 2, 3′ dianhydride with Arthrobacter ureafaciens. J. Biochem. 78 (1975) 1201–1206. [DOI] [PMID: 1225919]
2.  Neubauer, A., Walter, M., and Buchholz, K. Formation of inulobiose from difructoseanhydride III catalysed by a lysate from Arthrobacter ureafaciens ATCC 21124. Biocatalysis and Biotransformation 18 (2000) 443–455. [DOI]
3.  Saito, K., Sumita, Y., Nagasaka, Y., Tomita, F. and Yokota, A. Molecular cloning of the gene encoding the di-D-fructofuranose 1,2′:2,3′ dianhydride hydrolysis enzyme (DFA IIIase) from Arthrobacter sp. H65-7. J. Biosci. Bioeng. 95 (2003) 538–540. [DOI] [PMID: 16233453]
4.  Yu, S., Wang, X., Zhang, T., Stressler, T., Fischer, L., Jiang, B. and Mu, W. Identification of a novel di-D-fructofuranose 1,2′:2,3′ dianhydride (DFA III) hydrolysis enzyme from Arthrobacter aurescens SK8.001. PLoS One 10:e0142640 (2015). [DOI] [PMID: 26555784]
5.  Yu, S., Shen, H., Cheng, Y., Zhu, Y., Li, X., and Mu, W. Structural and functional basis of difructose anhydride III hydrolase, which sequentially converts inulin using the same catalytic residue. ACS Catalysis 8 (2018) 10683–10697. [DOI]
[EC 4.2.1.178 created 2021]
 
 
EC 3.2.1.64     Relevance: 36.5%
Accepted name: 2,6-β-fructan 6-levanbiohydrolase
Reaction: Hydrolysis of (2→6)-β-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(β-D-fructofuranosyl)-D-fructose, from the end of the chain
Other name(s): β-2,6-fructan-6-levanbiohydrolase; 2,6-β-D-fructan 6-levanbiohydrolase; levanbiose-producing levanase; 2,6-β-D-fructan 6-β-D-fructofuranosylfructohydrolase
Systematic name: (2→6)-β-D-fructofuranan 6-(β-D-fructosyl)-D-fructose-hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-46-3
References:
1.  Avigad, G. and Zelikson, R. Cleavage of fructans to levanbiose by a specific hydrolase. Bull. Res. Counc. Isr. 11 (1963) 253–257.
2.  Saito, K., Kondo, K., Kojima, I., Yokota, A. and Tomita, F. Purification and characterization of 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. Appl. Environ. Microbiol. 66 (2000) 252–256. [DOI] [PMID: 10618232]
3.  Saito, K., Oda, Y., Tomita, F. and Yokota, A. Molecular cloning of the gene for 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. FEMS Microbiol. Lett. 218 (2003) 265–270. [DOI] [PMID: 12586402]
4.  Song, E.K., Kim, H., Sung, H.K. and Cha, J. Cloning and characterization of a levanbiohydrolase from Microbacterium laevaniformans ATCC 15953. Gene 291 (2002) 45–55. [DOI] [PMID: 12095678]
5.  Kang, E.J., Lee, S.O., Lee, J.D., Lee, T.H. and Lee, T.H. Purification and characterization of a levanbiose-producing levanase from Pseudomonas sp. No. 43. Biotechnol. Appl. Biochem. 29 (1999) 263–268. [PMID: 10334957]
[EC 3.2.1.64 created 1972, modified 2004]
 
 
EC 6.1.2.2     Relevance: 35.8%
Accepted name: nebramycin 5′ synthase
Reaction: (1) tobramycin + carbamoyl phosphate + ATP + H2O = nebramycin 5′ + AMP + diphosphate + phosphate (overall reaction)
(1a) carbamoyl phosphate + ATP + H2O = diphosphate + O-carbamoyladenylate + phosphate
(1b) O-carbamoyladenylate + tobramycin = AMP + nebramycin 5′
(2) kanamycin A + carbamoyl phosphate + ATP + H2O = 6′′-O-carbamoylkanamycin A + AMP + diphosphate + phosphate (overall reaction)
(2a) carbamoyl phosphate + ATP + H2O = diphosphate + O-carbamoyladenylate + phosphate
(2b) O-carbamoyladenylate + kanamycin A = AMP + 6′′-O-carbamoylkanamycin A
For diagram of kanamycin A biosynthesis, click here
Glossary: tobramycin = (1S,2S,3R,4S,6R)-4,6-diamino-3-(2,6-diamino-2,3,6-trideoxy-α-D-ribo-hexopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
nebramycin 5′ = (1S,2S,3R,4S,6R)-4,6-diamino-3-[(2,6-diamino-2,3,6-trideoxy-α-D-ribo-hexopyranosyl)oxy]-2-hydroxycyclohexyl 3-amino-6-O-carbamoyl-3-deoxy-α-D-glucopyranoside
kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy--D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy--D-glucopyranoside
6′′-O-carbamoylkanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-[(6-amino-6-deoxy-α-D-glucopyranosyl)oxy]-2-hydroxycyclohexyl 3-amino-6-O-carbamoyl-3-deoxy-α-D-glucopyranoside
Other name(s): tobramycin carbamoyltransferase; TobZ
Systematic name: tobramycin:carbamoyl phosphate ligase (AMP,phosphate-forming)
Comments: Requires Fe(III). The enzyme from the bacterium Streptoalloteichus tenebrarius catalyses the activation of carbamoyl phosphate to O-carbamoyladenylate and the subsequent carbamoylation of kanamycin and tobramycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Parthier, C., Gorlich, S., Jaenecke, F., Breithaupt, C., Brauer, U., Fandrich, U., Clausnitzer, D., Wehmeier, U.F., Bottcher, C., Scheel, D. and Stubbs, M.T. The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic reaction. Angew. Chem. Int. Ed. Engl. 51 (2012) 4046–4052. [DOI] [PMID: 22383337]
[EC 6.1.2.2 created 2014]
 
 
EC 1.1.1.355     Relevance: 35.7%
Accepted name: 2′-dehydrokanamycin reductase
Reaction: kanamycin A + NADP+ = 2′-dehydrokanamycin A + NADPH + H+
For diagram of kanamycin A biosynthesis, click here
Glossary: kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
2′-dehydrokanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-[(6-amino-6-deoxy-α-D-arabino-hexopyranosyl-2-ulose)oxy]-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
Other name(s): kanK (gene name, ambiguous)
Systematic name: kanamycin A:NADP+ oxidoreductase
Comments: Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of kanamycin B to kanamycin A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sucipto, H., Kudo, F. and Eguchi, T. The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the α-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK. Angew. Chem. Int. Ed. Engl. 51 (2012) 3428–3431. [DOI] [PMID: 22374809]
[EC 1.1.1.355 created 2013]
 
 
EC 5.4.99.15     Relevance: 35%
Accepted name: (1→4)-α-D-glucan 1-α-D-glucosylmutase
Reaction: 4-[(1→4)-α-D-glucosyl]n-1-D-glucose = 1-α-D-[(1→4)-α-D-glucosyl]n-1-α-D-glucopyranoside
Other name(s): malto-oligosyltrehalose synthase; maltodextrin α-D-glucosyltransferase
Systematic name: (1→4)-α-D-glucan 1-α-D-glucosylmutase
Comments: The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1→4)-α-D-glucans containing three or more (1→4)-α-linked D-glucose units. Not active towards maltose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 170780-49-1
References:
1.  Maruta, K., Nakada, T., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Formation of trehalose from maltooligosaccharides by a novel enzymatic system. Biosci. Biotechnol. Biochem. 59 (1995) 1829–1834. [DOI] [PMID: 8534970]
2.  Nakada, T., Maruta, K., Tsusaki, K., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36. Biosci. Biotechnol. Biochem. 59 (1995) 2210–2214. [PMID: 8611744]
3.  Nakada, T., Ikegami, S., Chaen, H., Kubota, M., Fukuda, S., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biosci. Biotechnol. Biochem. 60 (1996) 263–266. [DOI] [PMID: 9063973]
[EC 5.4.99.15 created 1999]
 
 
EC 1.14.11.52     Relevance: 34%
Accepted name: validamycin A dioxygenase
Reaction: validamycin A + 2-oxoglutarate + O2 = validamycin B + succinate + CO2
For diagram of validamycin biosynthesis, click here
Glossary: validamycin A = (1R,2R,3S,4S,6R)-2,3-dihydroxy-6-(hydroxymethyl)-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}cyclohexyl β-D-glucopyranoside
validamycin B = (1R,2R,3S,4S,5R,6S)-2,3,5-trihydroxy-6-(hydroxymethyl)-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}cyclohexyl β-D-glucopyranoside
Other name(s): vldW (gene name)
Systematic name: validamycin-A,2-oxoglutarate:oxygen oxidoreductase (6′-hydroxylating)
Comments: The enzyme was characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Almabruk, K.H., Asamizu, S., Chang, A., Varghese, S.G. and Mahmud, T. The α-ketoglutarate/Fe(II)-dependent dioxygenase VldW is responsible for the formation of validamycin B. ChemBioChem 13 (2012) 2209–2211. [DOI] [PMID: 22961651]
[EC 1.14.11.52 created 2016]
 
 
EC 2.4.1.267     Relevance: 33.9%
Accepted name: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG6; Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; 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
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
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 α-1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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. [DOI] [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. [DOI] [PMID: 14517965]
[EC 2.4.1.267 created 2011, modified 2012]
 
 
EC 2.4.1.265     Relevance: 33.3%
Accepted name: dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG8; Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; 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
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
Comments: The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [PMID: 12480927]
[EC 2.4.1.265 created 2011, modified 2012]
 
 
EC 4.1.2.65     Relevance: 32.5%
Accepted name: ferulate hydratase/lyase
Reaction: ferulate + H2O = vanillin + acetate (overall reaction)
(1a) ferulate + H2O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate
(1b) 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate = vanillin + acetate
Glossary: ferulate = 4-hydroxy-3-methoxycinnamate
vanillin = 4-hydroxy-3-methoxybenzaldehyde
Other name(s): vanillin synthase; VpVan; VAN; ferulate aldolase
Systematic name: ferulate acetate-lyase (vanillin-forming)
Comments: The enzyme is located in the chloroplasts of vanilla pods of the orchid Vanilla planifolia. It also converts ferulic acid 4-O-β-D-glucopyranoside to vanillin 4-O-β-D-glucopyranoside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gallage, N.J., Hansen, E.H., Kannangara, R., Olsen, C.E., Motawia, M.S., Jørgensen, K., Holme, I., Hebelstrup, K., Grisoni, M. and Møller, B.L. Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. Nat. Commun. 5:4037 (2014). [DOI] [PMID: 24941968]
2.  Kundu, A. Vanillin biosynthetic pathways in plants. Planta 245 (2017) 1069–1078. [DOI] [PMID: 28357540]
3.  Gallage, N.J., Jørgensen, K., Janfelt, C., Nielsen, A.JZ., Naake, T., Dunski, E., Dalsten, L., Grisoni, M. and Møller, B.L. The intracellular localization of the vanillin biosynthetic machinery in pods of Vanilla planifolia. Plant Cell Physiol. 59 (2018) 304–318. [DOI] [PMID: 29186560]
[EC 4.1.2.65 created 2024]
 
 
EC 2.4.1.256     Relevance: 32.4%
Accepted name: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = dolichyl phosphate + α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase; 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 2-α-D-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol α-1,2-glucosyltransferase (configuration-retaining)
Comments: This eukaryotic 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. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 9597543]
[EC 2.4.1.256 created 2011, modified 2012]
 
 
EC 3.2.1.207     Relevance: 31.9%
Accepted name: mannosyl-oligosaccharide α-1,3-glucosidase
Reaction: (1) Glc2Man9GlcNAc2-[protein] + H2O = GlcMan9GlcNAc2-[protein] + β-D-glucopyranose
(2) GlcMan9GlcNAc2-[protein] + H2O = Man9GlcNAc2-[protein] + β-D-glucopyranose
Glossary: Glc2Man9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein]
GlcMan9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein]
Man9GlcNAc2-[protein] = {α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein]
Other name(s): ER glucosidase II; α-glucosidase II; trimming glucosidase II; ROT2 (gene name); GTB1 (gene name); GANAB (gene name); PRKCSH (gene name)
Systematic name: Glc2Man9GlcNAc2-[protein] 3-α-glucohydrolase (configuration-inverting)
Comments: This eukaryotic enzyme cleaves off sequentially the two α-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Trombetta, E.S., Simons, J.F. and Helenius, A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 271 (1996) 27509–27516. [DOI] [PMID: 8910335]
2.  Ziak, M., Meier, M., Etter, K.S. and Roth, J. Two isoforms of trimming glucosidase II exist in mammalian tissues and cell lines but not in yeast and insect cells. Biochem. Biophys. Res. Commun. 280 (2001) 363–367. [DOI] [PMID: 11162524]
3.  Wilkinson, B.M., Purswani, J. and Stirling, C.J. Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J. Biol. Chem. 281 (2006) 6325–6333. [DOI] [PMID: 16373354]
4.  Mora-Montes, H.M., Bates, S., Netea, M.G., Diaz-Jimenez, D.F., Lopez-Romero, E., Zinker, S., Ponce-Noyola, P., Kullberg, B.J., Brown, A.J., Odds, F.C., Flores-Carreon, A. and Gow, N.A. Endoplasmic reticulum α-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction. Eukaryot Cell 6 (2007) 2184–2193. [DOI] [PMID: 17933909]
[EC 3.2.1.207 created 2018]
 
 
EC 2.4.1.260     Relevance: 31.3%
Accepted name: dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-α-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, 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; Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase; 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
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-inverting)
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, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 12217961]
[EC 2.4.1.260 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.160, modified 2012]
 
 
EC 2.8.2.37     Relevance: 31%
Accepted name: trehalose 2-sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + α,α-trehalose = adenosine 3′,5′-bisphosphate + 2-O-sulfo-α,α-trehalose
Glossary: 2-O-sulfo-α,α-trehalose = trehalose 2-sulfate = α-D-glucopyranosyl 2-O-sulfo-α-D-glucopyranoside
Other name(s): Stf0 sulfotransferase; 3′-phosphoadenylyl-sulfate:α,α-trehalose 2-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:α,α-trehalose 2-sulfonotransferase
Comments: The sulfation of trehalose in the bacterium Mycobacterium tuberculosis is required for the biosynthesis of sulfolipid-1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mougous, J.D., Petzold, C.J., Senaratne, R.H., Lee, D.H., Akey, D.L., Lin, F.L., Munchel, S.E., Pratt, M.R., Riley, L.W., Leary, J.A., Berger, J.M. and Bertozzi, C.R. Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 11 (2004) 721–729. [DOI] [PMID: 15258569]
2.  Pi, N., Hoang, M.B., Gao, H., Mougous, J.D., Bertozzi, C.R. and Leary, J.A. Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrometry. Anal. Biochem. 341 (2005) 94–104. [DOI] [PMID: 15866533]
[EC 2.8.2.37 created 2014]
 
 
EC 2.4.1.367     Relevance: 30.8%
Accepted name: ginsenoside 6-O-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + protopanaxatriol = UDP + ginsenoside Rh1
(2) UDP-α-D-glucose + ginsenoside F1 = UDP + (20S)-ginsenoside Rg1
Glossary: protopanaxatriol = (3β,6α,12β)-dammar-24-ene-3,6,12,20-tetrol
ginsenoside F1 = (3β,6α,12β)-trihydroxydammar-24-en-20-yl β-D-glucopyranoside
Other name(s): UGTPg100 (gene name)
Systematic name: UDP-α-D-glucose:ginsenoside 6-O-glucosyltransferase
Comments: The enzyme, characterized from the plant Panax ginseng, glucosylates the C-6 position of protopanaxatriol and ginsenoside F1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412–1424. [PMID: 26032089]
[EC 2.4.1.367 created 2019]
 
 
EC 2.4.1.364     Relevance: 30.3%
Accepted name: protopanaxadiol-type ginsenoside 3-O-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + (20S)-protopanaxadiol = UDP + (20S)-ginsenoside Rh2
(2) UDP-α-D-glucose + ginsenoside C-K = UDP + ginsenoside F2
Glossary: (20S)-protopanaxadiol = (3β,12β)-dammar-24-ene-3,12,20-triol
ginsenoside C-K = (3β,12β)-3,12-dihydroxydammar-24-en-20-yl β-D-glucopyranoside
Other name(s): UGT74AE2 (gene name)
Systematic name: UDP-α-D-glucose:protopanaxadiol-type ginsenoside 3-O-glucosyltransferase (configuration-retaining)
Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C-3-OH group of (20S)-protopanaxadiol and ginsenoside C-K.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jung, S.C., Kim, W., Park, S.C., Jeong, J., Park, M.K., Lim, S., Lee, Y., Im, W.T., Lee, J.H., Choi, G. and Kim, S.C. Two ginseng UDP-glycosyltransferases synthesize ginsenoside Rg3 and Rd. Plant Cell Physiol. 55 (2014) 2177–2188. [PMID: 25320211]
[EC 2.4.1.364 created 2019]
 
 
EC 2.4.1.261     Relevance: 30.3%
Accepted name: dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase; 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 2-α-D-mannosyltransferase
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting)
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, MetaCyc
References:
1.  Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910–917. [DOI] [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. [DOI] [PMID: 15987956]
[EC 2.4.1.261 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.261, modified 2012]
 
 
EC 3.2.1.122     Relevance: 29.9%
Accepted name: maltose-6′-phosphate glucosidase
Reaction: α-maltose 6′-phosphate + H2O = D-glucose + D-glucose 6-phosphate
Other name(s): phospho-α-glucosidase; maltose-6′-phosphate 6-phosphoglucohydrolase
Systematic name: α-maltose-6′-phosphate 6-phosphoglucohydrolase
Comments: Hydrolyses a variety of 6-phospho-α-D-glucosides, including α-maltose 6′-phosphate, α,α-trehalose 6-phosphate, sucrose 6-phosphate and p-nitrophenyl-α-D-glucopyranoside 6-phosphate (as a chromogenic substrate). The enzyme is activated by FeII, MnII, CoII and NiII. It is rapidly inactivated in air.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 98445-08-0
References:
1.  Thompson, J., Gentry-Weeks, C.R., Nguyen, N.Y., Folk, J.E., Robrish, S.A. Purification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-α-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyses maltose 6-phosphate and related phospho-α-D-glucosides. J. Bacteriol. 177 (1995) 2505–2512. [DOI] [PMID: 7730284]
[EC 3.2.1.122 created 1989, modified 1999]
 
 
EC 3.2.1.106     Relevance: 29.7%
Accepted name: mannosyl-oligosaccharide glucosidase
Reaction: Glc3Man9GlcNAc2-[protein] + H2O = Glc2Man9GlcNAc2-[protein] + β-D-glucopyranose
Glossary: Glc3Man9GlcNAc2 = [α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Glc2Man9GlcNAc2-[protein] = [α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Other name(s): Glc3Man9NAc2 oligosaccharide glucosidase; trimming glucosidase I; CWH41 (gene name); MOGS (gene name); mannosyl-oligosaccharide glucohydrolase
Systematic name: Glc3Man9GlcNAc2-[protein] glucohydrolase (configuration-inverting)
Comments: This enzyme catalyses the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal α-1,2-linked glucose residue. This and subsequent processing steps are required before complex N-glycans can be synthesized.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 78413-07-7
References:
1.  Elting, J.J., Chen, W.W. and Lennarz, J. Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains. J. Biol. Chem. 255 (1980) 2325–2331. [PMID: 7358674]
2.  Grinna, L.S. and Robbins, P.W. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J. Biol. Chem. 254 (1979) 8814–8818. [PMID: 479161]
3.  Kilker, R.D., Saunier, B., Tkacz, J.S. and Herscovics, A. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J. Biol. Chem. 256 (1981) 5299–5603. [PMID: 7014569]
4.  Grinna, L.S. and Robbins, P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255 (1980) 2255–2258. [PMID: 7358666]
5.  Mark, M.J. and Kornfeld, S. Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch. Biochem. Biophys. 199 (1980) 249–258. [DOI] [PMID: 7356331]
[EC 3.2.1.106 created 1984, modified 2018]
 
 
EC 2.4.1.155     Relevance: 29.6%
Accepted name: α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here
Other name(s): MGAT5 (gene name); N-acetylglucosaminyltransferase V; α-mannoside β-1,6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-mannoside β1→6-acetylglucosaminyltransferase; UDP-N-acetylglucosamine:α-mannoside-β1,6 N-acetylglucosaminyltransferase; α-1,3(6)-mannosylglycoprotein β-1,6-N-acetylglucosaminyltransferase; GnTV; GlcNAc-T V; UDP-N-acetyl-D-glucosamine:6-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)-β-D-mannosyl-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires Mg2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. It catalyses the addition of N-acetylglucosamine in β 1-6 linkage to the α-linked mannose of biantennary N-linked oligosaccharides, and thus enables the synthesis of tri- and tetra-antennary complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83588-90-3
References:
1.  Cummings, R.D., Trowbridge, I.S. and Kornfeld, S. A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: α-D-mannoside β1,6 N-acetylglucosaminyltransferase. J. Biol. Chem. 257 (1982) 13421–13427. [PMID: 6216250]
2.  Hindsgaul, O., Tahir, S.H., Srivastava, O.P. and Pierce, M. The trisaccharide β-D-GlcpNAc-(1→2)-α-D-Manp-(1→6)-β-D-Manp, as its 8-methoxycarbonyloctyl glycoside, is an acceptor selective for N-acetylglucosaminyltransferase V. Carbohydr. Res. 173 (1988) 263–272. [DOI] [PMID: 2834054]
3.  Shoreibah, M.G., Hindsgaul, O. and Pierce, M. Purification and characterization of rat kidney UDP-N-acetylglucosamine: α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 267 (1992) 2920–2927. [PMID: 1531335]
4.  Gu, J., Nishikawa, A., Tsuruoka, N., Ohno, M., Yamaguchi, N., Kangawa, K. and Taniguchi, N. Purification and characterization of UDP-N-acetylglucosamine: α-6-D-mannoside β 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line. J. Biochem. 113 (1993) 614–619. [PMID: 8393437]
5.  Park, C., Jin, U.H., Lee, Y.C., Cho, T.J. and Kim, C.H. Characterization of UDP-N-acetylglucosamine:α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B. Arch. Biochem. Biophys. 367 (1999) 281–288. [PMID: 10395745]
6.  Saito, T., Miyoshi, E., Sasai, K., Nakano, N., Eguchi, H., Honke, K. and Taniguchi, N. A secreted type of β 1,6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase activity. J. Biol. Chem. 277 (2002) 17002–17008. [PMID: 11872751]
[EC 2.4.1.155 created 1986, modified 2001, modified 2018]
 
 
EC 2.4.1.259     Relevance: 29.5%
Accepted name: dolichyl-P-Man:Man6GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man6GlcNAc2-PP-Dol α-1,2-mannosyltransferase; 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
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting)
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, MetaCyc
References:
1.  Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910–917. [DOI] [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. [DOI] [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. [DOI] [PMID: 15987956]
[EC 2.4.1.259 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.259, modified 2012]
 
 
EC 2.4.99.22      
Transferred entry: N-acetylglucosaminide α-(2,6)-sialyltransferase. Now EC 2.4.3.10, N-acetylglucosaminide α-(2,6)-sialyltransferase
[EC 2.4.99.22 created 2020, deleted 2022]
 
 
EC 2.4.3.10     Relevance: 29.4%
Accepted name: N-acetylglucosaminide α-(2,6)-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-β-D-glucosaminyl-R
Other name(s): α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylglucosaminide 6-α-sialyltransferase; N-acetylglucosaminide (α 2→6)-sialyltransferase; ST6GlcNAc
Systematic name: CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminide N-acetyl-β-D-glucosamine-6-α-N-acetylneuraminyltransferase (configuration-inverting)
Comments: Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetyl-β-D-glucosamine. The enzyme from rat liver also acts on β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl residues, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Paulson, J.C., Weinstein, J. and de Souza-e-Silva, U. Biosynthesis of a disialylated sequence in N-linked oligosaccharides: identification of an N-acetylglucosaminide (α 2→6)-sialyltransferase in Golgi apparatus from rat liver. Eur. J. Biochem. 140 (1984) 523–530. [PMID: 6547092]
[EC 2.4.3.10 created 2020 as EC 2.4.99.22, transferred 2022 to EC 2.4.3.10]
 
 
EC 2.4.1.264     Relevance: 29.2%
Accepted name: D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 2-β-glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + α-D-Man-(1→3)-β-D-Glc-(1→4)-α-D-Glc-1-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-GlcA-(1→2)-α-D-Man-(1→3)-β-D-Glc-(1→4)-α-D-Glc-1-diphospho-ditrans,octacis-undecaprenol
For diagram of xanthan biosynthesis, click here
Other name(s): GumK; UDP-glucuronate:D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol β-1,2-glucuronyltransferase; D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 2-β-glucuronyltransferase
Systematic name: UDP-α-D-glucuronate:α-D-Man-(1→3)-β-D-Glc-(1→4)-α-D-Glc-1-diphospho-ditrans,octacis-undecaprenol β-1,2-glucuronosyltransferase (configuration-inverting)
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, MetaCyc, PDB
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 14736729]
[EC 2.4.1.264 created 2011, modified 2016]
 
 
EC 2.4.1.145     Relevance: 29%
Accepted name: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): N-acetylglucosaminyltransferase IV; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; β-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-glycopeptide β4-acetylglucosaminyltransferase IV; α-1,3-mannosylglycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTIV; UDP-N-acetyl-D-glucosamine:3-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires Mn2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 86498-16-0
References:
1.  Gleeson, P.A. and Schachter, H. Control of glycoprotein synthesis. J. Biol. Chem. 258 (1983) 6162–6173. [PMID: 6222042]
2.  Oguri, S., Minowa, M.T., Ihara, Y., Taniguchi, N., Ikenaga, H. and Takeuchi, M. Purification and characterization of UDP-N-acetylglucosamine: α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase-IV) from bovine small intestine. J. Biol. Chem. 272 (1997) 22721–22727. [DOI] [PMID: 9278430]
3.  Minowa, M.T., Oguri, S., Yoshida, A., Hara, T., Iwamatsu, A., Ikenaga, H. and Takeuchi, M. cDNA cloning and expression of bovine UDP-N-acetylglucosamine: α1, 3-D-mannoside β1,4-N-acetylglucosaminyltransferase IV. J. Biol. Chem. 273 (1998) 11556–11562. [DOI] [PMID: 9565571]
4.  Yoshida, A., Minowa, M.T., Takamatsu, S., Hara, T., Oguri, S., Ikenaga, H. and Takeuchi, M. Tissue specific expression and chromosomal mapping of a human UDP-N-acetylglucosamine: α1,3-d-mannoside β1, 4-N-acetylglucosaminyltransferase. Glycobiology 9 (1999) 303–310. [DOI] [PMID: 10024668]
5.  Yoshida, A., Minowa, M.T., Takamatsu, S., Hara, T., Ikenaga, H. and Takeuchi, M. A novel second isoenzyme of the human UDP-N-acetylglucosamine:α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment. Glycoconj. J. 15 (1998) 1115–1123. [PMID: 10372966]
6.  Takamatsu, S., Antonopoulos, A., Ohtsubo, K., Ditto, D., Chiba, Y., Le, D.T., Morris, H.R., Haslam, S.M., Dell, A., Marth, J.D. and Taniguchi, N. Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice. Glycobiology 20 (2010) 485–497. [DOI] [PMID: 20015870]
[EC 2.4.1.145 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 2.5.1.98     Relevance: 28.9%
Accepted name: Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase
Reaction: phosphoenolpyruvate + [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n = [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→3)-4,6-CH3(COO-)C-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n + phosphate
Other name(s): PssM; phosphoenolpyruvate:[D-GlcA-β-(1→4)-2-O-Ac-D-GlcA-β-(1→4)-D-Glc-β-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-D-Gal-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→6)]-2(or 3)-O-Ac-D-Glc-α-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Systematic name: phosphoenolpyruvate:[β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Comments: The enzyme is responsible for pyruvylation of the subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ivashina, T.V., Fedorova, E.E., Ashina, N.P., Kalinchuk, N.A., Druzhinina, T.N., Shashkov, A.S., Shibaev, V.N. and Ksenzenko, V.N. Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciae—Pisum sativum symbiosis. J. Appl. Microbiol. 109 (2010) 731–742. [DOI] [PMID: 20233262]
[EC 2.5.1.98 created 2012, modified 2018]
 
 
EC 2.4.1.363     Relevance: 28.8%
Accepted name: ginsenoside 20-O-glucosyltransferase
Reaction: UDP-α-D-glucose + (20S)-protopanaxadiol = UDP + ginsenoside C-K
Glossary: (20S)-protopanaxadiol = (3β,12β)-dammar-24-ene-3,12,20-triol
ginsenoside C-K = (3β,12β)-3,12-dihydroxydammar-24-en-20-yl β-D-glucopyranoside
Other name(s): UGT71A27 (gene name)
Systematic name: UDP-α-D-glucose:(20S)-protopanaxadiol 20-O-glucosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C20(S)-OH group of dammarane derivative substrates, including protopanaxatriol, dammarenediol II, (20S)-ginsenoside Rh2, and (20S)-ginsenoside Rg3. It does not act on the 20R epimer of protopanaxadiol, or on ginsenosides that are glucosylated at the C-6 position, such as ginsenoside Rh1 or ginsenoside Rg2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yan, X., Fan, Y., Wei, W., Wang, P., Liu, Q., Wei, Y., Zhang, L., Zhao, G., Yue, J. and Zhou, Z. Production of bioactive ginsenoside compound K in metabolically engineered yeast. Cell Res. 24 (2014) 770–773. [PMID: 24603359]
2.  Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412–1424. [PMID: 26032089]
[EC 2.4.1.363 created 2019]
 
 
EC 2.4.1.201     Relevance: 28.7%
Accepted name: α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here
Other name(s): MGAT4C (gene name); N-acetylglucosaminyltransferase VI; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI; uridine diphosphoacetylglucosamine-glycopeptide β-1→4-acetylglucosaminyltransferase VI; mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTVI; GlcNAc-T VI; UDP-N-acetyl-D-glucosamine:2,6-bis(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→2)]-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires a high concentration of Mn2+ for maximal activity. The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus. It transfers GlcNAc in β1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by β linkages. No homologous enzyme appears to exist in mammals.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119699-68-2
References:
1.  Brockhausen, I., Hull, E., Hindsgaul, O., Schachter, H., Shah, R.N., Michnick, S.W. and Carver, J.P. Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc β1-6 (GlcNAc β1-2)Man α-R (GlcNAc to Man) β-4-N-acetylglucosaminyltransferase VI. J. Biol. Chem. 264 (1989) 11211–11221. [PMID: 2525556]
2.  Taguchi, T., Ogawa, T., Inoue, S., Inoue, Y., Sakamoto, Y., Korekane, H. and Taniguchi, N. Purification and characterization of UDP-GlcNAc:GlcNAcβ1-6(GlcNAcβ1-2)Manα1-R [GlcNAc to Man]-β1,4-N-acetylglucosaminyltransferase VI from hen oviduct. J. Biol. Chem. 275 (2000) 32598–32602. [DOI] [PMID: 10903319]
3.  Sakamoto, Y., Taguchi, T., Honke, K., Korekane, H., Watanabe, H., Tano, Y., Dohmae, N., Takio, K., Horii, A. and Taniguchi, N. Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcβ 1-6(GlcNAcβ 1-2)- manα 1-R[GlcNAc to man]β 1,4N-acetylglucosaminyltransferase VI. J. Biol. Chem. 275 (2000) 36029–36034. [DOI] [PMID: 10962001]
[EC 2.4.1.201 created 1992, modified 2001, modified 2018]
 
 


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