KEGG   ENZYME: 1.14.19.69
Entry
EC 1.14.19.69               Enzyme                                 

Name
biflaviolin synthase;
CYP158A2 (gene name);
cytochrome P450 158A2
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
Sysname
flaviolin,reduced ferredoxin:oxygen oxidoreductase
Reaction(IUBMB)
(1) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,3'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O [RN:R08912];
(2) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,8'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O [RN:R08913]
Reaction(KEGG)
R08912 R08913
Substrate
flaviolin [CPD:C18012];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
3,3'-biflaviolin [CPD:C18013];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
H2O [CPD:C00001];
3,8'-biflaviolin [CPD:C18014]
Comment
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].
History
EC 1.14.19.69 created 2008 as EC 1.14.21.7, transferred 2018 to EC 1.14.19.69
Orthology
K13074  biflaviolin synthase
K19628  biflaviolin synthase
Genes
SCO: SCO1207(2SCG58.07) SCO6998(SC8F11.24c)
SMA: SAVERM_7130(cyp25)
SHY: SHJG_2646 SHJG_6732
SHO: SHJGH_2410 SHJGH_6492
SCT: SCAT_5028
SCY: SCATT_50200
SVE: SVEN_0292 SVEN_5366
SDV: BN159_1508 BN159_7378(cyp25)
SCI: B446_03420 B446_06315 B446_31265
SLV: SLIV_04255 SLIV_31760
SGM: GCM10017557_72050(cyp158a2)
SEN: SACE_1242(cyp25)
 » show all
Reference
1  [PMID:15659395]
  Authors
Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR
  Title
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2.
  Journal
J Biol Chem 280:11599-607 (2005)
DOI:10.1074/jbc.M410933200
  Sequence
[sco:SCO1207]
Reference
2  [PMID:16239228]
  Authors
Zhao B, Guengerich FP, Voehler M, Waterman MR
  Title
Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer.
  Journal
J Biol Chem 280:42188-97 (2005)
DOI:10.1074/jbc.M509220200
  Sequence
[sco:SCO1207]
Reference
3  [PMID:17614370]
  Authors
Zhao B, Lamb DC, Lei L, Kelly SL, Yuan H, Hachey DL, Waterman MR
  Title
Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2.
  Journal
Biochemistry 46:8725-33 (2007)
DOI:10.1021/bi7006959
  Sequence
[sco:SCO6998]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.69
IUBMB Enzyme Nomenclature: 1.14.19.69
ExPASy - ENZYME nomenclature database: 1.14.19.69
BRENDA, the Enzyme Database: 1.14.19.69

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