The Enzyme Database

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EC 1.1.1.219     
Accepted name: dihydroflavonol 4-reductase
Reaction: a (2R,3S,4S)-leucoanthocyanidin + NADP+ = a (2R,3R)-dihydroflavonol + NADPH + H+
For diagram of flavonoid biosynthesis, click here
Other name(s): dihydrokaempferol 4-reductase; dihydromyricetin reductase; NADPH-dihydromyricetin reductase; dihydroquercetin reductase; DFR (gene name); cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase; dihydroflavanol 4-reductase (incorrect)
Systematic name: (2R,3S,4S)-leucoanthocyanidin:NADP+ 4-oxidoreductase
Comments: This plant enzyme, involved in the biosynthesis of anthocyanidins, is known to act on (+)-dihydrokaempferol, (+)-taxifolin, and (+)-dihydromyricetin, although some enzymes may act only on a subset of these compounds. Each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol. NAD+ can act instead of NADP+, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83682-99-9
References:
1.  Heller, W., Forkmann, G., Britsch, L. and Grisebach, H. Enzymatic reduction of (+)-dihydroflavonols to flavan-3,4-cis- diols with flower extracts from Matthiola incana and its role in anthocyanin biosynthesis. Planta 165 (1985) 284–287. [PMID: 24241054]
2.  Stafford, H.A. and Lester, H.H. Flavan-3-ol biosynthesis the conversion of (+)-dihydromyricetin to its flavan-3,4-diol (leucodelphinidin) and to (+)-gallocatechin by reductases extracted from tissue-cultures of Ginkgo biloba and Pseudotsuga-menziesii. Plant Physiol. 78 (1985) 791–794. [PMID: 16664326]
3.  Fischer, D., Stich, K., Britsch, L. and Grisebach, H. Purification and characterization of (+)dihydroflavonol (3-hydroxyflavanone) 4-reductase from flowers of Dahlia variabilis. Arch. Biochem. Biophys. 264 (1988) 40–47. [DOI] [PMID: 3293532]
4.  Li, H., Qiu, J., Chen, F., Lv, X., Fu, C., Zhao, D., Hua, X. and Zhao, Q. Molecular characterization and expression analysis of dihydroflavonol 4-reductase (DFR) gene in Saussurea medusa. Mol. Biol. Rep. 39 (2012) 2991–2999. [DOI] [PMID: 21701830]
[EC 1.1.1.219 created 1989, modified 2016]
 
 
EC 1.3.1.51     
Accepted name: 2′-hydroxydaidzein reductase
Reaction: 2′-hydroxy-2,3-dihydrodaidzein + NADP+ = 2′-hydroxydaidzein + NADPH + H+
For diagram of glyceollin biosynthesis (part 1), click here
Other name(s): NADPH:2′-hydroxydaidzein oxidoreductase; HDR; 2′-hydroxydihydrodaidzein:NADP+ 2′-oxidoreductase
Systematic name: 2′-hydroxy-2,3-dihydrodaidzein:NADP+ 2′-oxidoreductase
Comments: In the reverse reaction, the 2′-hydroxyisoflavone (2′-hydroxydaidzein) is reduced to an isoflavanone. Also acts on 2′-hydroxyformononetin and to a small extent on 2′-hydroxygenistein. Involved in the biosynthesis of the phytoalexin glyceollin. The isoflavones biochanin A, daidzein and genestein as well as the flavonoids apigenin, kaempferol and quercetin do not act as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 126125-01-7
References:
1.  Fischer, D., Ebenau-Jehle, C. and Grisebach, H. Phytoalexin synthesis in soybean: purification and characterization of NADPH:2′-hydroxydaidzein oxidoreductase from elicitor-challenged soybean cell cultures. Arch. Biochem. Biophys. 276 (1990) 390–395. [DOI] [PMID: 2306102]
[EC 1.3.1.51 created 1992, modified 2004]
 
 
EC 1.13.11.24     
Accepted name: quercetin 2,3-dioxygenase
Reaction: quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
For diagram of reaction, click here
Other name(s): quercetinase; flavonol 2,4-oxygenase; quercetin:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: quercetin:oxygen 2,3-oxidoreductase (ring-opening)
Comments: The enzyme from Aspergillus sp. is a copper protein whereas that from Bacillus subtilis contains iron. Quercetin is a flavonol (5,7,3′,4′-tetrahydroxyflavonol).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-67-6
References:
1.  Oka, T. and Simpson, F.J. Quercetinase, a dioxygenase containing copper. Biochem. Biophys. Res. Commun. 43 (1971) 1–5. [DOI] [PMID: 5579942]
2.  Steiner, R.A., Kalk, K.H. and Dijkstra, B.W. Anaerobic enzyme·substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA 99 (2002) 16625–16630. [DOI] [PMID: 12486225]
3.  Bowater, L., Fairhurst, S.A., Just, V.J. and Bornemann, S. Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase. FEBS Lett. 557 (2004) 45–48. [DOI] [PMID: 14741339]
[EC 1.13.11.24 created 1972]
 
 
EC 1.14.11.19      
Transferred entry: anthocyanidin synthase. Now EC 1.14.20.4, anthocyanidin synthase
[EC 1.14.11.19 created 2001, modified 2017, deleted 2018]
 
 
EC 1.14.13.19     
Accepted name: taxifolin 8-monooxygenase
Reaction: taxifolin + NAD(P)H + H+ + O2 = 2,3-dihydrogossypetin + NAD(P)+ + H2O
Other name(s): taxifolin hydroxylase
Systematic name: taxifolin,NAD(P)H:oxygen oxidoreductase (8-hydroxylating)
Comments: A flavoprotein, converting a flavanol into a flavanone. Also acts on fustin, but not on catechin, quercetin or mollisacidin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39307-19-2
References:
1.  Jeffrey, A.M., Knight, M. and Evans, W.C. The bacterial degradation of flavonoids. Hydroxylation of the A-ring of taxifolin by a soil pseudomonad. Biochem. J. 130 (1972) 373–381. [PMID: 4146277]
[EC 1.14.13.19 created 1976]
 
 
EC 1.14.13.88      
Transferred entry: flavanoid 3,5-hydroxylase. Now EC 1.14.14.81, flavanoid 3,5-hydroxylase
[EC 1.14.13.88 created 2004, deleted 2018]
 
 
EC 1.14.14.81     
Accepted name: flavanoid 3′,5′-hydroxylase
Reaction: a flavanone + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = a 3′,5′-dihydroxyflavanone + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 3′-hydroxyflavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′,5′-dihydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of myricetin biosynthesis, click here, for diagram of the biosynthesis of naringenin derivatives, click here and for diagram of flavonoid biosynthesis, click here
Other name(s): flavonoid 3′,5′-hydroxylase
Systematic name: flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′,5′-dihydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The 3′,5′-dihydroxyflavanone is formed via the 3′-hydroxyflavanone. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The enzyme catalyses the hydroxylation of 5,7,4′-trihydroxyflavanone (naringenin) at either the 3′ position to form eriodictyol or at both the 3′ and 5′ positions to form 5,7,3′,4′,5′-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyses the hydroxylation of 3,5,7,3′,4′-pentahydroxyflavanone (taxifolin) at the 5′ position, forming ampelopsin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94047-23-1
References:
1.  Menting, J., Scopes, R.K. and Stevenson, T.W. Characterization of flavonoid 3′,5′-hydroxylase in microsomal membrane fraction of Petunia hybrida flowers. Plant Physiol. 106 (1994) 633–642. [PMID: 12232356]
2.  Shimada, Y., Nakano-Shimada, R., Ohbayashi, M., Okinaka, Y., Kiyokawa, S. and Kikuchi, Y. Expression of chimeric P450 genes encoding flavonoid-3′, 5′-hydroxylase in transgenic tobacco and petunia plants1. FEBS Lett. 461 (1999) 241–245. [DOI] [PMID: 10567704]
3.  de Vetten, N., ter Horst, J., van Schaik, H.P., de Boer, A., Mol, J. and Koes, R. A cytochrome b5 is required for full activity of flavonoid 3′, 5′-hydroxylase, a cytochrome P450 involved in the formation of blue flower colors. Proc. Natl. Acad. Sci. USA 96 (1999) 778–783. [DOI] [PMID: 9892710]
[EC 1.14.14.81 created 2004 as EC 1.14.13.88, transferred 2018 to EC 1.14.14.81]
 
 
EC 1.14.20.4     
Accepted name: anthocyanidin synthase
Reaction: a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O (overall reaction)
(1a) a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = a (4S)- 2,3-dehydroflavan-3,4-diol + succinate + CO2 + H2O
(1b) a (4S)- 2,3-dehydroflavan-3,4-diol = an anthocyanidin + H2O
For diagram of anthocyanin biosynthesis, click here
Glossary: taxifolin = 3,4-dihydroquercitin
Other name(s): leucocyanidin oxygenase; leucocyanidin,2-oxoglutarate:oxygen oxidoreductase; ANS (gene name)
Systematic name: (2R,3S,4S)-leucoanthocyanidin,2-oxoglutarate:oxygen oxidoreductase
Comments: The enzyme requires iron(II) and ascorbate. It is involved in the pathway by which many flowering plants make anthocyanin flower pigments (glycosylated anthocyandins). The enzyme hydroxylates the C-3 carbon, followed by a trans diaxial elimination, forming a C-2,C-3 enol. The product loses a second water molecule to form anthocyanidins. When assayed in vitro, non-enzymic epimerization of the product can lead to formation of dihydroflavanols. Thus when the substrate is leucocyanidin, a mixture of (+)-taxifolin and (+)-epitaxifolin are formed. The enzyme can also oxidize the formed (+)-taxifolin to quercetin (cf. EC 1.14.20.6, flavonol synthase) [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 180984-01-4
References:
1.  Saito, K., Kobayashi, M., Gong, Z., Tanaka, Y. and Yamazaki, M. Direct evidence for anthocyanidin synthase as a 2-oxoglutarate-dependent oxygenase: molecular cloning and functional expression of cDNA from a red forma of Perilla frutescens. Plant J. 17 (1999) 181–190. [DOI] [PMID: 10074715]
2.  Turnbull, J.J., Sobey, W.J., Aplin, R.T., Hassan, A., Firmin, J.L., Schofield, C.J. and Prescott, A.G. Are anthocyanidins the immediate products of anthocyanidin synthase? Chem. Commun. (2000) 2473–2474.
3.  Wilmouth, R.C., Turnbull, J.J., Welford, R.W., Clifton, I.J., Prescott, A.G. and Schofield, C.J. Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana. Structure 10 (2002) 93–103. [DOI] [PMID: 11796114]
4.  Turnbull, J.J., Nagle, M.J., Seibel, J.F., Welford, R.W., Grant, G.H. and Schofield, C.J. The C-4 stereochemistry of leucocyanidin substrates for anthocyanidin synthase affects product selectivity. Bioorg. Med. Chem. Lett. 13 (2003) 3853–3857. [DOI] [PMID: 14552794]
5.  Wellmann, F., Griesser, M., Schwab, W., Martens, S., Eisenreich, W., Matern, U. and Lukacin, R. Anthocyanidin synthase from Gerbera hybrida catalyzes the conversion of (+)-catechin to cyanidin and a novel procyanidin. FEBS Lett. 580 (2006) 1642–1648. [DOI] [PMID: 16494872]
[EC 1.14.20.4 created 2001 as EC 1.14.11.19, transferred 2018 to EC 1.14.20.4]
 
 
EC 2.1.1.42     
Accepted name: flavone 3′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3′-hydroxyflavone = S-adenosyl-L-homocysteine + 3′-methoxyflavone
For diagram of luteolin biosynthesis click here
Other name(s): o-dihydric phenol methyltransferase; luteolin methyltransferase; luteolin 3′-O-methyltransferase; o-diphenol m-O-methyltransferase; o-dihydric phenol meta-O-methyltransferase; S-adenosylmethionine:flavone/flavonol 3′-O-methyltransferase; quercetin 3′-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:3′-hydroxyflavone 3′-O-methyltransferase
Comments: The enzyme prefers flavones with vicinal 3′,4′-dihydroxyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37205-55-3
References:
1.  Ebel, J., Hahlbrock, K. and Grisebach, H. Purification and properties of an o-dihydricphenol meta-O-methyltransferase from cell suspension cultures of parsley and its relation to flavonoid biosynthesis. Biochim. Biophys. Acta 268 (1972) 313–326. [DOI] [PMID: 5026305]
2.  Muzac, I., Wang, J., Anzellotti, D., Zhang, H. and Ibrahim, R.K. Functional expression of an Arabidopsis cDNA clone encoding a flavonol 3′-O-methyltransferase and characterization of the gene product. Arch. Biochem. Biophys. 375 (2000) 385–388. [DOI] [PMID: 10700397]
3.  Poulton, J.E., Hahlbrock, K. and Grisebach, H. O-Methylation of flavonoid substrates by a partially purified enzyme from soybean cell suspension cultures. Arch. Biochem. Biophys. 180 (1977) 543–549. [DOI] [PMID: 18099]
4.  Kim, B.G., Lee, H.J., Park, Y., Lim, Y. and Ahn, J.H. Characterization of an O-methyltransferase from soybean. Plant Physiol. Biochem. 44 (2006) 236–241. [DOI] [PMID: 16777424]
5.  Lee, Y.J., Kim, B.G., Chong, Y., Lim, Y. and Ahn, J.H. Cation dependent O-methyltransferases from rice. Planta 227 (2008) 641–647. [DOI] [PMID: 17943312]
[EC 2.1.1.42 created 1976, modified 2011]
 
 
EC 2.1.1.76     
Accepted name: quercetin 3-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3,5,7,3′,4′-pentahydroxyflavone = S-adenosyl-L-homocysteine + 3-methoxy-5,7,3′,4′-tetrahydroxyflavone
For diagram of the biosynthesis of methylated quercetin derivatives, click here
Other name(s): flavonol 3-O-methyltransferase; flavonoid 3-methyltransferase
Systematic name: S-adenosyl-L-methionine:3,5,7,3′,4′-pentahydroxyflavone 3-O-methyltransferase
Comments: Specific for quercetin. Related enzymes bring about the 3-O-methylation of other flavonols, such as galangin and kaempferol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81295-55-8
References:
1.  De Luca, V., Brunet, G., Khouri, H., Ibrahim, R. and Hrazdina, G. Flavonol 3-O-methyltransferase in plant-tissues. Z. Naturforsch. 37 (1982) 134–135.
2.  De Luca, V. and Ibrahim, R.K. Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. I. Partial purification and some properties of S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and 4′-O-methyltransferases. Arch. Biochem. Biophys. 238 (1985) 596–605. [DOI] [PMID: 3994393]
3.  De Luca, V. and Ibrahim, R.K. Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. II. Substrate interaction and product inhibition studies of flavonol 3-, 6-, and 4′-O-methyltransferases. Arch. Biochem. Biophys. 238 (1985) 606–618. [DOI] [PMID: 3994394]
4.  Ibrahim, R.K. and De Luca, V. Polymethylated flavonol synthesis is catalyzed by distinct O-methyltransferases. Naturwissenschaften 69 (1982) 41–42.
[EC 2.1.1.76 created 1984]
 
 
EC 2.1.1.82     
Accepted name: 3-methylquercetin 7-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 5,7,3′,4′-tetrahydroxy-3-methoxyflavone = S-adenosyl-L-homocysteine + 5,3′,4′-trihydroxy-3,7-dimethoxyflavone
For diagram of the biosynthesis of methylated quercetin derivatives, click here
Other name(s): flavonol 7-O-methyltransferase; flavonol 7-methyltransferase; 7-OMT; S-adenosyl-L-methionine:3′,4′,5,7-tetrahydroxy-3-methoxyflavone 7-O-methyltransferase; 3-methylquercitin 7-O-methyltransferase [mis-spelt]
Systematic name: S-adenosyl-L-methionine:5,7,3′,4′-tetrahydroxy-3-methoxyflavone 7-O-methyltransferase
Comments: Involved with EC 2.1.1.76 quercetin 3-O-methyltransferase and EC 2.1.1.83 3,7-dimethylquercetin 4′-O-methyltransferase in the methylation of quercetin to 3,7,4′-trimethylquercetin in Chrysosplenium americanum. Does not act on flavones, dihydroflavonols, or their glucosides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97089-67-3
References:
1.  De Luca, V. and Ibrahim, R.K. Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. I. Partial purification and some properties of S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and 4′-O-methyltransferases. Arch. Biochem. Biophys. 238 (1985) 596–605. [DOI] [PMID: 3994393]
[EC 2.1.1.82 created 1989]
 
 
EC 2.1.1.83     
Accepted name: 3,7-dimethylquercetin 4′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 5,3′,4′-trihydroxy-3,7-dimethoxyflavone = S-adenosyl-L-homocysteine + 5,3′-dihydroxy-3,7,4′-trimethoxyflavone
For diagram of the biosynthesis of methylated quercetin derivatives, click here
Other name(s): flavonol 4′-O-methyltransferase; flavonol 4′-methyltransferase; 4′-OMT; S-adenosyl-L-methionine:3′,4′,5-trihydroxy-3,7-dimethoxyflavone 4′-O-methyltransferase; 3,7-dimethylquercitin 4′-O-methyltransferase [mis-spelt]
Systematic name: S-adenosyl-L-methionine:5,3′,4′-trihydroxy-3,7-dimethoxyflavone 4′-O-methyltransferase
Comments: 3,7-Dimethylquercetagetin can also act as acceptor. Involved with EC 2.1.1.76 quercetin 3-O-methyltransferase and EC 2.1.1.82 3-methylquercetin 7-O-methyltransferase in the methylation of quercetin to 3,7,4′-trimethylquercetin in Chrysosplenium americanum. Does not act on flavones, dihydroflavonols, or their glucosides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96477-60-0
References:
1.  De Luca, V. and Ibrahim, R.K. Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. I. Partial purification and some properties of S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and 4′-O-methyltransferases. Arch. Biochem. Biophys. 238 (1985) 596–605. [DOI] [PMID: 3994393]
2.  De Luca, V. and Ibrahim, R.K. Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. II. Substrate interaction and product inhibition studies of flavonol 3-, 6-, and 4′-O-methyltransferases. Arch. Biochem. Biophys. 238 (1985) 606–618. [DOI] [PMID: 3994394]
[EC 2.1.1.83 created 1989]
 
 
EC 2.1.1.88     
Accepted name: 8-hydroxyquercetin 8-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3,5,7,8,3′,4′-hexahydroxyflavone = S-adenosyl-L-homocysteine + 3,5,7,3′,4′-pentahydroxy-8-methoxyflavone
Other name(s): flavonol 8-O-methyltransferase; flavonol 8-methyltransferase; S-adenosyl-L-methionine:3,3′,4′,5,7,8-hexahydroxyflavone 8-O-methyltransferase; 8-hydroxyquercitin 8-O-methyltransferase [mis-spelt]
Systematic name: S-adenosyl-L-methionine:3,5,7,8,3′,4′-hexahydroxyflavone 8-O-methyltransferase
Comments: Also acts on 8-hydroxykaempferol, but not on the glycosides of 8-hydroxyflavonols. An enzyme from the flower buds of Lotus corniculatus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99775-17-4
References:
1.  Jay, M., De Luca, V. and Ibrahim, R.K. Purification, properties and kinetic mechanism of flavonol 8-O-methyltransferase from Lotus corniculatus L. Eur. J. Biochem. 153 (1985) 321–325. [DOI] [PMID: 4076180]
[EC 2.1.1.88 created 1989]
 
 
EC 2.1.1.118     
Accepted name: columbamine O-methyltransferase
Reaction: S-adenosyl-L-methionine + columbamine = S-adenosyl-L-homocysteine + palmatine
For diagram of columbamine, palmatine and corydaline biosynthesis, click here
Systematic name: S-adenosyl-L-methionine:columbamine O-methyltransferase
Comments: The product of this reaction is a protoberberine alkaloid that is widely distributed in the plant kingdom. This enzyme is distinct in specificity from EC 2.1.1.88, 8-hydroxyquercetin 8-O-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 105843-76-3
References:
1.  Rueffer, M., Amann, M., Zenk, M.H. S-Adenosyl-L-methionine:columbamine O-methyltransferase, a compartmentalized enzyme in protoberberine biosynthesis. Plant Cell Reports 3 (1986) 182–185. [DOI]
[EC 2.1.1.118 created 1999]
 
 
EC 2.1.1.155     
Accepted name: kaempferol 4′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + kaempferol = S-adenosyl-L-homocysteine + kaempferide
For diagram of kaempferol biosynthesis, click here
Glossary: kaempferide = 3,5,7-trihydroxy-4′-methoxyflavone
Other name(s): S-adenosyl-L-methionine:flavonoid 4′-O-methyltransferase; F 4′-OMT
Systematic name: S-adenosyl-L-methionine:kaempferol 4′-O-methyltransferase
Comments: The enzyme acts on the hydroxy group in the 4′-position of some flavones, flavanones and isoflavones. Kaempferol, apigenin and kaempferol triglucoside are substrates, as is genistein, which reacts more slowly. Compounds with an hydroxy group in the 3′ and 4′ positions, such as quercetin and eriodictyol, do not act as substrates. Similar to EC 2.1.1.75, apigenin 4′-O-methyltransferase and EC 2.1.1.83, 3,7-dimethylquercetin 4′-O-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80747-20-2
References:
1.  Curir, P., Lanzotti, V., Dolci, M., Dolci, P., Pasini, C. and Tollin, G. Purification and properties of a new S-adenosyl-L-methionine:flavonoid 4′-O-methyltransferase from carnation (Dianthus caryophyllus L.). Eur. J. Biochem. 270 (2003) 3422–3431. [DOI] [PMID: 12899699]
[EC 2.1.1.155 created 2004]
 
 
EC 2.1.1.231     
Accepted name: flavonoid 4′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + a 4′-hydroxyflavanone = S-adenosyl-L-homocysteine + a 4′-methoxyflavanone
For diagram of naringenin methyl ethers biosynthesis, click here
Glossary: naringenin = 4′,5,7-trihydroxyflavan-4-one
Other name(s): SOMT-2; 4′-hydroxyisoflavone methyltransferase
Systematic name: S-adenosyl-L-methionine:flavonoid 4′-O-methyltransferase
Comments: The enzyme catalyses the 4′-methylation of naringenin. In vitro it catalyses the 4′-methylation of apigenin, quercetin, daidzein and genistein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kim, D.H., Kim, B.G., Lee, Y., Ryu, J.Y., Lim, Y., Hur, H.G. and Ahn, J.H. Regiospecific methylation of naringenin to ponciretin by soybean O-methyltransferase expressed in Escherichia coli. J. Biotechnol. 119 (2005) 155–162. [DOI] [PMID: 15961179]
[EC 2.1.1.231 created 2011]
 
 
EC 2.1.1.267     
Accepted name: flavonoid 3′,5′-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + a 3′-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3′-methoxyflavonoid
(2) S-adenosyl-L-methionine + a 5′-hydroxy-3′-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3′,5′-dimethoxyflavonoid
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
myricetin = 3,3′,4′,5,5′,7-hexahydroxyflavone
quercetin = 3,3′,4′,5,7-pentahydroxyflavone
Other name(s): AOMT; CrOMT2
Systematic name: S-adenosyl-L-methionine:flavonoid 3′-O-methyltransferase
Comments: Isolated from Vitis vinifera (grape) [2]. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cacace, S., Schröder, G., Wehinger, E., Strack, D., Schmidt, J. and Schröder, J. A flavonol O-methyltransferase from Catharanthus roseus performing two sequential methylations. Phytochemistry 62 (2003) 127–137. [DOI] [PMID: 12482447]
2.  Hugueney, P., Provenzano, S., Verries, C., Ferrandino, A., Meudec, E., Batelli, G., Merdinoglu, D., Cheynier, V., Schubert, A. and Ageorges, A. A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine. Plant Physiol. 150 (2009) 2057–2070. [DOI] [PMID: 19525322]
[EC 2.1.1.267 created 2013, modified 2014]
 
 
EC 2.1.1.374     
Accepted name: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase
Reaction: S-adenosyl-L-methionine + 2-heptyl-1-hydroxyquinolin-4(1H)-one = S-adenosyl-L-homocysteine + 2-heptyl-1-methoxyquinolin-4(1H)-one
Other name(s): htm (gene name)
Systematic name: S-adenosyl-L-methionine:2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase
Comments: The enzyme, found in mycobacteria, is a member of a family of heterocyclic toxin methyltransferases. It is involved in defense against several antimicrobial natural compounds and drugs. 4-Hydroxyquinolin-2(1H)-one, 2-heptylquinolin-4(1H)-one, 2-heptyl-3-hydroxyquinolin-4(1H)-one (the "Pseudomonas quinolone signal", PQS) and the flavonol quercetin are also O-methylated, albeit with lower activity [2]. The enzyme also N-methylates the bactericidal compound 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Warrier, T., Kapilashrami, K., Argyrou, A., Ioerger, T.R., Little, D., Murphy, K.C., Nandakumar, M., Park, S., Gold, B., Mi, J., Zhang, T., Meiler, E., Rees, M., Somersan-Karakaya, S., Porras-De Francisco, E., Martinez-Hoyos, M., Burns-Huang, K., Roberts, J., Ling, Y., Rhee, K.Y., Mendoza-Losana, A., Luo, M. and Nathan, C.F. N-methylation of a bactericidal compound as a resistance mechanism in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 113 (2016) E4523–E4530. [DOI] [PMID: 27432954]
2.  Sartor, P., Bock, J., Hennecke, U., Thierbach, S. and Fetzner, S. Modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-hydroxyquinolin-4(1H)-one and other secondary metabolites by methyltransferases from mycobacteria. FEBS J. (2020) . [DOI] [PMID: 33064871]
[EC 2.1.1.374 created 2020]
 
 
EC 2.3.1.116     
Accepted name: flavonol-3-O-β-glucoside O-malonyltransferase
Reaction: malonyl-CoA + flavonol 3-O-β-D-glucoside = CoA + flavonol 3-O-(6-O-malonyl-β-D-glucoside)
For diagram of the biosynthesis of quercetin 3-O-glycoside derivatives, click here
Other name(s): flavonol 3-O-glucoside malonyltransferase; MAT-3; malonyl-coenzyme A:flavonol-3-O-glucoside malonyltransferase
Systematic name: malonyl-CoA:flavonol-3-O-β-D-glucoside 6′′-O-malonyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 78413-11-3
References:
1.  Matern, U., Feser, C. and Hammer, D. Further characterization and regulation of malonyl-coenzyme A: flavonoid glucoside malonyltransferases from parsley cell suspension cultures. Arch. Biochem. Biophys. 226 (1983) 206–217. [DOI] [PMID: 6639051]
[EC 2.3.1.116 created 1989]
 
 
EC 2.4.1.91     
Accepted name: flavonol 3-O-glucosyltransferase
Reaction: UDP-glucose + a flavonol = UDP + a flavonol 3-O-β-D-glucoside
For diagram of kaempferol biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-glycoside derivatives, click here
Other name(s): GTI; uridine diphosphoglucose-flavonol 3-O-glucosyltransferase; UDP-glucose:flavonol 3-O-glucosyltransferase; UDPG:flavonoid-3-O-glucosyltransferase
Systematic name: UDP-glucose:flavonol 3-O-D-glucosyltransferase
Comments: Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside. Different from EC 2.4.1.81 (flavone 7-O-β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50812-18-5
References:
1.  Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587–599.
2.  Sutter, A. and Grisebach, H. UDP-glucose: flavonol 3-O-glucosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 309 (1973) 289–295. [DOI] [PMID: 4731963]
[EC 2.4.1.91 created 1976]
 
 
EC 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 oxygenase, 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, 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]
 
 
EC 2.4.1.159     
Accepted name: flavonol-3-O-glucoside L-rhamnosyltransferase
Reaction: UDP-β-L-rhamnose + a flavonol 3-O-β-D-glucoside = UDP + a flavonol 3-O-[α-L-rhamnosyl-(1→6)-β-D-glucoside]
For diagram of quercetin 3-O-Glycoside derivatives biosynthesis, click here
Glossary: UDP-β-L-rhamnose = UDP-6-deoxy-β-L-mannose
Other name(s): uridine diphosphorhamnose-flavonol 3-O-glucoside rhamnosyltransferase; UDP-rhamnose:flavonol 3-O-glucoside rhamnosyltransferase; UDP-L-rhamnose:flavonol-3-O-D-glucoside 6′′-O-L-rhamnosyltransferase
Systematic name: UDP-β-L-rhamnose:flavonol-3-O-β-D-glucoside 6′′-O-L-rhamnosyltransferase (configuration-inverting)
Comments: A configuration-inverting rhamnosyltransferase that converts flavonol 3-O-glucosides to 3-O-rutinosides. Also acts, more slowly, on rutin, quercetin 3-O-galactoside and flavonol 3-O-rhamnosides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83380-89-6
References:
1.  Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587–599.
2.  Jones, P., Messner, B., Nakajima, J., Schaffner, A.R. and Saito, K. UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside biosynthesis in Arabidopsis thaliana. J. Biol. Chem. 278 (2003) 43910–43918. [DOI] [PMID: 12900416]
[EC 2.4.1.159 created 1986, modified 2015]
 
 
EC 2.4.1.234     
Accepted name: kaempferol 3-O-galactosyltransferase
Reaction: UDP-α-D-galactose + kaempferol = UDP + kaempferol 3-O-β-D-galactoside
For diagram of kaempferol biosynthesis, click here
Other name(s): F3GalTase; UDP-galactose:kaempferol 3-O-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:kaempferol 3-O-β-D-galactosyltransferase
Comments: Acts on the endogenous flavonols kaempferol and quercetin, to a lesser extent on myricetin and fisetin, and weakly on galangin and isorhamnetin. The reaction can occur equally well in both directions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Miller, K.D., Guyon, V., Evans, J.N., Shuttleworth, W.A. and Taylor, L.P. Purification, cloning, and heterologous expression of a catalytically efficient flavonol 3-O-galactosyltransferase expressed in the male gametophyte of Petunia hybrida. J. Biol. Chem. 274 (1999) 34011–34019. [DOI] [PMID: 10567367]
[EC 2.4.1.234 created 2004]
 
 
EC 2.4.1.237     
Accepted name: flavonol 7-O-β-glucosyltransferase
Reaction: UDP-glucose + a flavonol = UDP + a flavonol 7-O-β-D-glucoside
For diagram of quercetin 7-O-Glycoside biosynthesis, click here
Other name(s): UDP-glucose:flavonol 7-O-glucosyltransferase
Systematic name: UDP-glucose:flavonol 7-O-β-D-glucosyltransferase
Comments: Acts on the flavonols gossypetin (8-hydroxyquercetin) and to a lesser extent on quercetin, kaempferol and myricetin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-90-0
References:
1.  Stich, K., Halbwirth, H., Wurst, F. and Forkmann, G. UDP-glucose: flavonol 7-O-glucosyltransferase activity in flower extracts of Chrysanthemum segetum. Z. Naturforsch. C 52 (1997) 153–158. [PMID: 9167271]
[EC 2.4.1.237 created 2004]
 
 
EC 2.4.1.239     
Accepted name: flavonol-3-O-glucoside glucosyltransferase
Reaction: UDP-glucose + a flavonol 3-O-β-D-glucoside = UDP + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucoside
For diagram of kaempferol-glycoside biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-triglucoside, click here
Other name(s): UDP-glucose:flavonol-3-O-glucoside 2′′-O-β-D-glucosyltransferase
Systematic name: UDP-glucose:flavonol-3-O-β-D-glucoside 2′′-O-β-D-glucosyltransferase
Comments: One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a β-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91, flavonol 3-O-glucosyltransferase and EC 2.4.1.240, flavonol-3-O-glycoside glucosyltransferase). TDP-glucose can replace UDP-glucose as the glucose donor but the reaction proceeds more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jourdan, P.S. and Mansell, R.L. Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. Arch. Biochem. Biophys. 213 (1982) 434–443. [DOI] [PMID: 6462109]
[EC 2.4.1.239 created 2004]
 
 
EC 2.4.1.240     
Accepted name: flavonol-3-O-glycoside glucosyltransferase
Reaction: UDP-glucose + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucoside = UDP + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside
For diagram of kaempferol-glycoside biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-triglucoside, click here
Systematic name: UDP-glucose:flavonol-3-O-β-D-glucosyl-(1→2)-β-D-glucoside 2′′′-O-β-D-glucosyltransferase
Comments: One of three specific glucosyltransferases in pea (Pisum sativum) thatsuccessively add a β-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 flavonol 3-O-glucosyltransferase, and EC 2.4.1.239 flavonol-3-O-glucoside glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jourdan, P.S. and Mansell, R.L. Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. Arch. Biochem. Biophys. 213 (1982) 434–443. [DOI] [PMID: 6462109]
[EC 2.4.1.240 created 2004]
 
 
EC 2.4.2.35     
Accepted name: flavonol-3-O-glycoside xylosyltransferase
Reaction: UDP-α-D-xylose + a flavonol 3-O-glycoside = UDP + a flavonol 3-[β-D-xylosyl-(1→2)-β-D-glycoside]
For diagram of quercetin 3-o-glycoside derivatives biosynthesis, click here
Other name(s): UDP-D-xylose:flavonol-3-O-glycoside 2′′-O-β-D-xylosyltransferase
Systematic name: UDP-α-D-xylose:flavonol-3-O-glycoside 2′′-O-β-D-xylosyltransferase
Comments: Flavonol 3-O-glucoside, flavonol 3-O-galactoside and, more slowly, rutin, can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83380-90-9
References:
1.  Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587–599.
[EC 2.4.2.35 created 1986, modified 2014]
 
 
EC 2.4.2.51     
Accepted name: anthocyanidin 3-O-glucoside 2′′′-O-xylosyltransferase
Reaction: UDP-α-D-xylose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-β-D-sambubioside
For diagram of anthocyanidin sambubioside biosynthesis, click here
Glossary: anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)
Other name(s): uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase; UGT79B1
Systematic name: UDP-α-D-xylose:anthocyanidin-3-O-β-D-glucoside 2′′′-O-xylosyltransferase
Comments: Isolated from the plants Matthiola incana (stock) [1] and Arabidopsis thaliana (mouse-eared cress) [2]. The enzyme has similar activity with the 3-glucosides of pelargonidin, cyanidin, delphinidin, quercetin and kaempferol as well as with cyanidin 3-O-rhamnosyl-(1→6)-glucoside and cyanidin 3-O-(6-acylglucoside). There is no activity with other UDP-sugars or with cyanidin 3,5-diglucoside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Teusch, M. Uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase from petals of Matthiola incana R.Br. Planta 169 (1986) 559–563. [PMID: 24232765]
2.  Yonekura-Sakakibara, K., Fukushima, A., Nakabayashi, R., Hanada, K., Matsuda, F., Sugawara, S., Inoue, E., Kuromori, T., Ito, T., Shinozaki, K., Wangwattana, B., Yamazaki, M. and Saito, K. Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J. 69 (2012) 154–167. [DOI] [PMID: 21899608]
[EC 2.4.2.51 created 2013]
 
 
EC 2.4.2.56     
Accepted name: kaempferol 3-O-xylosyltransferase
Reaction: UDP-α-D-xylose + kaempferol = UDP + kaempferol 3-O-β-D-xyloside
For diagram of kaempferol biosynthesis, click here
Other name(s): F3XT; UDP-D-xylose:flavonol 3-O-xylosyltransferase; flavonol 3-O-xylosyltransferase
Systematic name: UDP-α-D-xylose:kaempferol 3-O-D-xylosyltransferase
Comments: The enzyme from the plant Euonymus alatus also catalyses the 3-O-D-xylosylation of other flavonols (e.g. quercetin, isorhamnetin, rhamnetin, myricetin, fisetin) with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ishikura, N. and Yang, Z.Q. UDP-D-xylose: flavonol 3-O-xylosyltransferase from young leaves of Euonymus alatus f. ciliato-dentatus. Z. Naturforsch. C: Biosci. 46 (1991) 1003–1010.
[EC 2.4.2.56 created 2013]
 
 
EC 2.8.2.22     
Accepted name: aryl-sulfate sulfotransferase
Reaction: an aryl sulfate + a phenol = a phenol + an aryl sulfate
Other name(s): arylsulfate-phenol sulfotransferase; arylsulfotransferase (ambiguous); ASST; arylsulfate sulfotransferase; arylsulfate:phenol sulfotransferase; astA (gene name); aryl-sulfate:phenol sulfotransferase
Systematic name: aryl-sulfate:phenol sulfonotransferase
Comments: The enzyme, characterized from bacteria that colonize the human and mouse intestine, catalyses the transfer of a sulfate group from a phenol sulfate ester to other phenolic compounds. Activity is enhanced by Mg2+ and Mn2+ [1]. Unlike EC 2.8.2.9, tyrosine-ester sulfotransferase and EC 2.8.2.1, aryl sulfotransferase, the enzyme does not act on 3′-phosphoadenylyl sulfate or adenosine 3′,5′-bisphosphate [1].The level of sulfation of polyphenols depends on the positions of the hydroxyl groups [3-5]. Hydroxy groups of tyrosine residues in peptides such as angiotensin can also act as acceptors [2]. The reaction proceeds according to a ping pong bi bi mechanism [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 158254-86-5
References:
1.  Kim, D.-H., Konishi, L. and Kobashi, K. Purification, characterization and reaction mechanism of novel arylsulfotransferase obtained from an anaerobic bacterium of human intestine. Biochim. Biophys. Acta 872 (1986) 33–41. [DOI] [PMID: 3460636]
2.  Kobashi, K., Kim, D.-H. and Morikawa, T. A novel type of arylsulfotransferase. J. Protein Chem. 6 (1987) 237–244.
3.  Koizumi, M., Shimizu, M. and Kobashi, K. Enzymatic sulfation of quercetin by arylsulfotransferase from a human intestinal bacterium. Chem Pharm Bull (Tokyo) 38 (1990) 794–796. [PMID: 2347024]
4.  Koizumi, M., Akao, T., Kadota, S., Kikuchi, T., Okuda, T. and Kobashi, K. Enzymatic sulfation of polyphenols related to tannins by arylsulfotransferase. Chem Pharm Bull (Tokyo) 39 (1991) 2638–2643. [PMID: 1806284]
5.  Konishi-Imamura, L., Sato, M., Dohi, K., Kadota, S., Namba, T. and Kobashi, K. Enzymatic sulfation of glycosides and their corresponding aglycones by arylsulfate sulfotransferase from a human intestinal bacterium. Biol. Pharm. Bull. 17 (1994) 1018–1022. [PMID: 7820100]
6.  Lee, N.S., Kim, B.T., Kim, D.H. and Kobashi, K. Purification and reaction mechanism of arylsulfate sulfotransferase from Haemophilus K-12, a mouse intestinal bacterium. J. Biochem. 118 (1995) 796–801. [PMID: 8576095]
7.  Kim, B., Hyun, Y.J., Lee, K.S., Kobashi, K. and Kim, D.H. Cloning, expression and purification of arylsulfate sulfotransferase from Eubacterium A-44. Biol. Pharm. Bull. 30 (2007) 11–14. [PMID: 17202651]
[EC 2.8.2.22 created 1990]
 
 
EC 2.8.2.25     
Accepted name: flavonol 3-sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + quercetin = adenosine 3′,5′-bisphosphate + quercetin 3-sulfate
For diagram of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): 3′-phosphoadenylyl-sulfate:quercetin 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin 3-sulfonotransferase
Comments: Also acts on some other flavonol aglycones.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 121855-10-5
References:
1.  Varin, L. and Ibrahim, R.K. Partial purification and characterization of 3 flavonol-specific sulfotransferases from Flaveria chloraefolia. Plant Physiol. 90 (1989) 977–981. [PMID: 16666908]
[EC 2.8.2.25 created 1992]
 
 
EC 2.8.2.26     
Accepted name: quercetin-3-sulfate 3′-sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3′,5′-bisphosphate + quercetin 3,3′-bissulfate
For diagram of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): flavonol 3′-sulfotransferase; 3′-Sulfotransferase; PAPS:flavonol 3-sulfate 3′-sulfotransferase; 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 3′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 3′-sulfonotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 121855-11-6
References:
1.  Varin, L. and Ibrahim, R.K. Partial purification and characterization of 3 flavonol-specific sulfotransferases from Flaveria chloraefolia. Plant Physiol. 90 (1989) 977–981. [PMID: 16666908]
[EC 2.8.2.26 created 1992]
 
 
EC 2.8.2.27     
Accepted name: quercetin-3-sulfate 4′-sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3′,5′-bisphosphate + quercetin 3,4′-bissulfate
For diagram of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): flavonol 4′-sulfotransferase; PAPS:flavonol 3-sulfate 4′-sulfotransferase; 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 4′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin-3-sulfate 4′-sulfonotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 121855-12-7
References:
1.  Varin, L. and Ibrahim, R.K. Partial purification and characterization of 3 flavonol-specific sulfotransferases from Flaveria chloraefolia. Plant Physiol. 90 (1989) 977–981. [PMID: 16666908]
[EC 2.8.2.27 created 1992]
 
 
EC 2.8.2.28     
Accepted name: quercetin-3,3′-bissulfate 7-sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + quercetin 3,3′-bissulfate = adenosine 3′,5′-bisphosphate + quercetin 3,7,3′-trissulfate
For diagram of sulfated quercetin derivatives biosynthesis, click here
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): flavonol 7-sulfotransferase; 7-sulfotransferase; PAPS:flavonol 3,3′/3,4′-disulfate 7-sulfotransferase; 3′-phosphoadenylyl-sulfate:quercetin-3,3′-bissulfate 7-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:quercetin-3,3′-bissulfate 7-sulfonotransferase
Comments: Quercetin 3,4′-bissulfate can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 121855-13-8
References:
1.  Varin, L. Enzymatic synthesis of sulfated flavonoids in Flaveria spp. Bull. Liaison-Groupe Polyphenols 14 (1988) 248–257.
[EC 2.8.2.28 created 1992]
 
 
EC 3.2.1.66      
Deleted entry: The activity is covered by EC 3.2.1.40, α-L-rhamnosidase
[EC 3.2.1.66 created 1972, deleted 2021]
 
 


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