ExplorEnz: EC 2.4.1.11*

Your query returned 11 entries. Printable version

2.4.1.11

Accepted name:

glycogen(starch) synthase

Reaction:

UDP-α-D-glucose + [(1→4)-α-D-glucosyl]_n = UDP + [(1→4)-α-D-glucosyl]_n+1

For diagram of glycogen, click here

Other name(s):

UDP-glucose—glycogen glucosyltransferase; glycogen (starch) synthetase; UDP-glucose-glycogen glucosyltransferase; UDP-glycogen synthase; UDPG-glycogen synthetase; UDPG-glycogen transglucosylase; uridine diphosphoglucose-glycogen glucosyltransferase; UDP-glucose:glycogen 4-α-D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:glycogen 4-α-D-glucosyltransferase (configuration-retaining)

Comments:

The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, glycogen phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose [EC 2.4.1.21, starch synthase (glycosyl-transferring)].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9014-56-6

References:

1.	Algranati, I.D. and Cabib, E. The synthesis of glycogen in yeast. Biochim. Biophys. Acta 43 (1960) 141–142. [DOI] [PMID: 13682402]
2.	Basu, D.K. and Bachhawat, B.K. Purification of uridine diphosphoglucose-glycogen transglucosylase from sheep brain. Biochim. Biophys. Acta 50 (1961) 123–128. [DOI] [PMID: 13687710]
3.	Leloir, L.F. and Cardini, C.E. UDPG-glycogen transglucosylase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 317–326.
4.	Leloir, L.F. and Goldemberg, S.H. Synthesis of glycogen from uridine diphosphate glucose in liver. J. Biol. Chem. 235 (1960) 919–923. [PMID: 14415527]
5.	Pitcher, J., Smythe, C. and Cohen, P. Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle. Eur. J. Biochem. 176 (1988) 391–395. [DOI] [PMID: 2970965]

[EC 2.4.1.11 created 1961]

2.4.1.110

Accepted name:

tRNA-queuosine α-mannosyltransferase

Reaction:

GDP-α-D-mannose + queuosine³⁴ in tRNA^Asp = GDP + O-4′′-α-D-mannosylqueuosine³⁴ in tRNA^Asp

Other name(s):

GDP-mannose:tRNA^Asp-queuosine O-5′′-β-D-mannosyltransferase (incorrect); tRNA-queuosine β-mannosyltransferase (incorrect)

Systematic name:

GDP-α-D-mannose:queuosine³⁴ in tRNA^Asp O-4′′-α-D-mannosyltransferase (configuration-retaining)

Comments:

This enzyme, found in higher vertebrates, modifies tRNA^Asp at the wobble position of the anticodon loop.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9055-06-5

References:

1.	Okada, N. and Nishimura, S. Enzymatic synthesis of Q nucleoside containing mannose in the anticodon of tRNA: isolation of a novel mannosyltransferase from a cell-free extract of rat liver. Nucleic Acids Res. 4 (1977) 2931–2938. [DOI] [PMID: 20603]
2.	Hillmeier, M., Wagner, M., Ensfelder, T., Korytiakova, E., Thumbs, P., Muller, M. and Carell, T. Synthesis and structure elucidation of the human tRNA nucleoside mannosyl-queuosine. Nat. Commun. 12:7123 (2021). [DOI] [PMID: 34880214]

[EC 2.4.1.110 created 1984, modified 2022]

2.4.1.111

Accepted name:

coniferyl-alcohol glucosyltransferase

Reaction:

UDP-glucose + coniferyl alcohol = UDP + coniferin

Other name(s):

uridine diphosphoglucose-coniferyl alcohol glucosyltransferase; UDP-glucose coniferyl alcohol glucosyltransferase

Systematic name:

UDP-glucose:coniferyl-alcohol 4′-β-D-glucosyltransferase

Comments:

Sinapyl alcohol can also act as acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61116-23-2

References:

1.	Ibrahim, R.K. and Grisebach, H. Purification and properties of UDP-glucose: coniferyl alcohol glucosyltransferase from suspension cultures of Paul's scarlet rose. Arch. Biochem. Biophys. 176 (1976) 700–708. [DOI] [PMID: 10853]

[EC 2.4.1.111 created 1984]

2.4.1.112

Deleted entry:

α-1,4-glucan-protein synthase (UDP-forming). The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase

[EC 2.4.1.112 created 1984, deleted 2007]

2.4.1.113

Accepted name:

α-1,4-glucan-protein synthase (ADP-forming)

Reaction:

ADP-glucose + protein = ADP + α-D-glucosyl-protein

Other name(s):

ADP-glucose:protein glucosyltransferase; adenosine diphosphoglucose-protein glucosyltransferase

Systematic name:

ADP-glucose:protein 4-α-D-glucosyltransferase

Comments:

The enzyme builds up α-1,4-glucan chains covalently bound to protein, thus acting as an initiator of glycogen synthesis.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67053-99-0

References:

1.	Barengo, R. and Krisman, C.R. Initiation of glycogen biosynthesis in Escherichia coli. Studies of the properties of the enzymes involved. Biochim. Biophys. Acta 540 (1978) 190–196. [DOI] [PMID: 418819]

[EC 2.4.1.113 created 1984]

2.4.1.114

Accepted name:

2-coumarate O-β-glucosyltransferase

Reaction:

UDP-glucose + trans-2-hydroxycinnamate = UDP + trans-β-D-glucosyl-2-hydroxycinnamate

Other name(s):

uridine diphosphoglucose-o-coumarate glucosyltransferase; UDPG:o-coumaric acid O-glucosyltransferase

Systematic name:

UDP-glucose:trans-2-hydroxycinnamate O-β-D-glucosyltransferase

Comments:

Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73665-97-1

References:

1.	Kleinhofs, A., Haskins, F.A. and Gorz, H.J. trans-o-Hydroxylcinnamic acid glucosylation in cell-free extracts of Melilotus alba. Phytochemistry 6 (1967) 1313–1318.
2.	Poulton, J.E., McRee, B.E. and Conn, E.E. Intracellular localization of two enzymes involved in coumarin biosynthesis in Melilotus alba. Plant Physiol. 65 (1980) 171–175. [PMID: 16661155]

[EC 2.4.1.114 created 1984]

2.4.1.115

Accepted name:

anthocyanidin 3-O-glucosyltransferase

Reaction:

UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-β-D-glucoside

For diagram of anthocyanin biosynthesis, click here

Other name(s):

uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase; UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-glucosyltransferase; UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase; 3-GT

Systematic name:

UDP-D-glucose:anthocyanidin 3-O-β-D-glucosyltransferase

Comments:

The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.20.4, anthocyanidin synthase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself [3].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 65607-32-1

References:

1.	Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1045–1058. [PMID: 751640]
2.	Ford, C.M., Boss, P.K. and Høj, P.B. Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo. J. Biol. Chem. 273 (1998) 9224–9233. [DOI] [PMID: 9535914]
3.	Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis. J. Biol. Chem. 276 (2001) 25797–25803. [DOI] [PMID: 11316805]

[EC 2.4.1.115 created 1984 (EC 2.4.1.233 created 2004, incorporated 2005), modified 2005]

2.4.1.116

Accepted name:

cyanidin 3-O-rutinoside 5-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + cyanidin-3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-β-D-glucoside

For diagram of anthocyanidin rutoside biosynthesis, click here

Glossary:

cyanidin 3-O-rutinoside = cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase; cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside 5-O-D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside 5-O-β-D-glucosyltransferase

Comments:

Isolated from the plants Silene dioica (red campion) [1], Iris ensata (Japanese iris) [2] and Iris hollandica (Dutch iris) [3]. Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 70248-66-7

References:

1.	Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1059–1071. [PMID: 751641]
2.	Yabuya, T., Yamaguchi, M., Imayama, T., Katoh, K. and Ino I. Anthocyanin 5-O-glucosyltransferase in flowers of Iris ensata. Plant Sci. 162 (2002) 779–784.
3.	Imayama, T., Yoshihara, Y., Fukuchi-Mizutani, M., Tanaka, Y., Ino, I. and Yabuya, T. Isolation and characterization of a cDNA clone of UDP-glucose:anthocyanin 5-O-glucosyltransferase in Iris hollandica. Plant Sci. 167 (2004) 1243–1248.

[EC 2.4.1.116 created 1984 (EC 2.4.1.235 created 2004, incorporated 2006), modified 2006, modified 2013]

2.4.1.117

Accepted name:

dolichyl-phosphate β-glucosyltransferase

Reaction:

UDP-α-D-glucose + dolichyl phosphate = UDP + dolichyl β-D-glucosyl phosphate

Other name(s):

polyprenyl phosphate:UDP-D-glucose glucosyltransferase; UDP-glucose dolichyl-phosphate glucosyltransferase; uridine diphosphoglucose-dolichol glucosyltransferase; UDP-glucose:dolichol phosphate glucosyltransferase; UDP-glucose:dolicholphosphoryl glucosyltransferase; UDP-glucose:dolichyl monophosphate glucosyltransferase; UDP-glucose:dolichyl phosphate glucosyltransferase; UDP-glucose:dolichyl-phosphate β-D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:dolichyl-phosphate β-D-glucosyltransferase (configuration-inverting)

Comments:

Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 71061-42-2

References:

1.	Behrens, N.H. and Leloir, L.F. Dolichol monophosphate glucose: an intermediate in glucose transfer in liver. Proc. Natl. Acad. Sci. USA 66 (1970) 153–159. [DOI] [PMID: 5273893]
2.	Herscovics, A., Bugge, B. and Jeanloz, R.W. Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose. J. Biol. Chem. 252 (1977) 2271–2277. [PMID: 849929]
3.	Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate: UDP-D-glucose glucosyltransferase. J. Biol. Chem. 254 (1979) 4814–4819. [PMID: 438216]

[EC 2.4.1.117 created 1984]

2.4.1.118

Accepted name:

cytokinin 7-β-glucosyltransferase

Reaction:

UDP-glucose + an N⁶-alkylaminopurine = UDP + an N⁶-alkylaminopurine-7-β-D-glucoside

Glossary:

zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N⁶-(4-hydroxy-3-methylbut-2-enyl)adenine

Other name(s):

uridine diphosphoglucose-zeatin 7-glucosyltransferase; cytokinin 7-glucosyltransferase; UDP-glucose:zeatin 7-glucosyltransferase

Systematic name:

UDP-glucose:N⁶-alkylaminopurine 7-glucosyltransferase

Comments:

Acts on a range of N⁶-substituted adenines, including zeatin and N⁶-benzylaminopurine, but not N⁶-benzyladenine. With some acceptors, 9-β-D-glucosides are also formed.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72103-03-8

References:

1.	Entsch, B. and Letham, D.S. Enzymic glucosylation of the cytokinin, 6-benzylaminopurine. Plant Sci. Lett. 14 (1979) 205–212.
2.	Entsch, B., Parker, C.W., Letham, D.S. and Summons, R.E. Preparation and characterization, using high-performance liquid chromatography, of an enzyme forming glucosides of cytokinins. Biochim. Biophys. Acta 570 (1979) 124–139. [DOI] [PMID: 486500]

[EC 2.4.1.118 created 1984]

2.4.1.119

Transferred entry:

dolichyl-diphosphooligosaccharideprotein glycotransferase. As the enzyme transfers more than one hexosyl group, it has been transferred to EC 2.4.99.18, dolichyl-diphosphooligosaccharideprotein glycotransferase

[EC 2.4.1.119 created 1984, deleted 2012]