EC |
1.14.19.69 |
Accepted name: |
biflaviolin synthase |
Reaction: |
(1) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,3′-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (2) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,8′-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Glossary: |
flaviolin = 4,5,7-trihydroxynaphthalene-1,2-dione
3,3′-biflaviolin = 3,3′,6,6′,8,8′-hexahydroxy-2,2′-binaphthalene-1,1′,4,4′-tetraone
3,8′-biflaviolin = 2,3′,4,6′,7,8′-hexahydroxy-1,2′-binaphthalene-1′,4′,5,8-tetraone |
Other name(s): |
CYP158A2 (gene name); cytochrome P450 158A2 |
Systematic name: |
flaviolin,reduced ferredoxin:oxygen oxidoreductase |
Comments: |
This cytochrome-P-450 (heme-thiolate) enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product [1,3]. The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation [1]. |
References: |
1. |
Zhao, B., Guengerich, F.P., Bellamine, A., Lamb, D.C., Izumikawa, M., Lei, L., Podust, L.M., Sundaramoorthy, M., Kalaitzis, J.A., Reddy, L.M., Kelly, S.L., Moore, B.S., Stec, D., Voehler, M., Falck, J.R., Shimada, T. and Waterman, M.R. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J. Biol. Chem. 280 (2005) 11599–11607. [PMID: 15659395] |
2. |
Zhao, B., Guengerich, F.P., Voehler, M. and Waterman, M.R. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J. Biol. Chem. 280 (2005) 42188–42197. [PMID: 16239228] |
3. |
Zhao, B., Lamb, D.C., Lei, L., Kelly, S.L., Yuan, H., Hachey, D.L. and Waterman, M.R. Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry 46 (2007) 8725–8733. [PMID: 17614370] |
|
[EC 1.14.19.69 created 2008 as EC 1.14.21.7, transferred 2018 to EC 1.14.19.69] |
|
|
|
|
EC
|
1.14.21.7
|
Transferred entry: | biflaviolin synthase. Now EC 1.14.19.69, biflaviolin synthase
|
[EC 1.14.21.7 created 2008, deleted 2018] |
|
|
|
|
EC |
2.5.1.123 |
Accepted name: |
flaviolin linalyltransferase |
Reaction: |
geranyl diphosphate + flaviolin = 3-linalylflaviolin + diphosphate |
Glossary: |
flaviolin = 2,5,7-trihydroxynaphthalene-1,4-dione
3-linalylflaviolin = 2,5,7-trihydroxy-3-(3,7-dimethylocta-1,6-dien-3-yl)naphthalene-1,4-dione |
Other name(s): |
Fnq26 |
Systematic name: |
geranyl-diphosphate:flaviolin 3-linalyltransferase |
Comments: |
Does not require Mg2+ or any other metal ions. Isolated from the bacterium Streptomyces cinnamonensis. In vitro the enzyme also forms traces of 3-geranylflaviolin. |
References: |
1. |
Haagen, Y., Unsold, I., Westrich, L., Gust, B., Richard, S.B., Noel, J.P. and Heide, L. A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates. FEBS Lett. 581 (2007) 2889–2893. [PMID: 17543953] |
|
[EC 2.5.1.123 created 2014] |
|
|
|
|
EC |
2.5.1.124 |
Accepted name: |
6-linalyl-2-O,3-dimethylflaviolin synthase |
Reaction: |
geranyl diphosphate + 2-O,3-dimethylflaviolin = diphosphate + 6-linalyl-2-O,3-dimethylflaviolin |
Glossary: |
flaviolin = 2,5,7-trihydroxy-1,4-naphthoquinone
2-O,3-dimethylflaviolin = 5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
6-linalyl-2-O,3-dimethylflaviolin = 6-(3,7-dimethylocta-1,6-dien-3-yl)-5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione |
Other name(s): |
Fur7; 6-(3,7-dimethylocta-1,6-dien-3-yl)-5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase |
Systematic name: |
geranyl-diphosphate:2-O-methyl-3-methylflaviolin geranyltransferase (6-linalyl-2-O,3-dimethylflaviolin-forming) |
Comments: |
The enzyme is involved in biosynthesis of the polyketide-isoprenoid furaquinocin D in the bacterium Streptomyces sp. KO-3988. It catalyses the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 6-linalyl-2-O,3-dimethylflaviolin and 7-O-geranyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.125, 7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase) in a 10:1 ratio. |
References: |
1. |
Kumano, T., Tomita, T., Nishiyama, M. and Kuzuyama, T. Functional characterization of the promiscuous prenyltransferase responsible for furaquinocin biosynthesis: identification of a physiological polyketide substrate and its prenylated reaction products. J. Biol. Chem. 285 (2010) 39663–39671. [PMID: 20937800] |
|
[EC 2.5.1.124 created 2014] |
|
|
|
|
EC |
2.5.1.125 |
Accepted name: |
7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase |
Reaction: |
geranyl diphosphate + 2-O,3-dimethylflaviolin = diphosphate + 7-O-geranyl-2-O,3-dimethylflaviolin
|
Glossary: |
flaviolin = 2,5,7-trihydroxy-1,4-naphthoquinone
2-O,3-dimethylflaviolin = 5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
7-O-geranyl-2-O,3-dimethylflaviolin = 7-{[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy}-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione |
Other name(s): |
Fur7 |
Systematic name: |
geranyl-diphosphate:2-O,3-dimethylflaviolin geranyltransferase (7-O-geranyl-2-O,3-dimethylflaviolin-forming) |
Comments: |
The enzyme is involved in furaquinocin biosynthesis in the bacterium Streptomyces sp. KO-3988. It catalyses the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 7-O-geranyl-2-O,3-dimethylflaviolin and 6-linalyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.124, 6-linalyl-2-O,3-dimethylflaviolin synthase) in a 1:10 ratio. |
References: |
1. |
Kumano, T., Tomita, T., Nishiyama, M. and Kuzuyama, T. Functional characterization of the promiscuous prenyltransferase responsible for furaquinocin biosynthesis: identification of a physiological polyketide substrate and its prenylated reaction products. J. Biol. Chem. 285 (2010) 39663–39671. [PMID: 20937800] |
|
[EC 2.5.1.125 created 2014] |
|
|
|
|