KEGG   ENZYME: 1.14.21.7Help
Entry
EC 1.14.21.7                Enzyme                                 

Name
biflaviolin synthase;
CYP158A2;
CYP 158A2;
cytochrome P450 158A2
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and the other dehydrogenated
BRITE hierarchy
Sysname
flaviolin,NADPH:oxygen oxidoreductase
Reaction(IUBMB)
(1) 2 flaviolin + NADPH + H+ + O2 = 3,3'-biflaviolin + NADP+ + 2 H2O [RN:R08912];
(2) 2 flaviolin + NADPH + H+ + O2 = 3,8'-biflaviolin + NADP+ + 2 H2O [RN:R08913]
Reaction(KEGG)
Substrate
flaviolin [CPD:C18012];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
3,3'-biflaviolin [CPD:C18013];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
3,8'-biflaviolin [CPD:C18014]
Comment
This cytochrome-P-450 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 1.14.21.7 created 2008
Orthology
K13074  biflaviolin synthase
K19628  biflaviolin synthase
Genes
SCO: SCO1207(2SCG58.07) SCO6998(SC8F11.24c)
SMA: SAVERM_1171(cyp5) SAVERM_7130(cyp25)
SGR: SGR_6619(p450-mel)
SGB: WQO_01990
SCT: SCAT_5028
SCY: SCATT_50200
SHY: SHJG_2265 SHJG_2646 SHJG_6732
SHO: SHJGH_2030 SHJGH_2410 SHJGH_6492
SVE: SVEN_0292 SVEN_5366
SDV: BN159_1508 BN159_7378(cyp25)
SALB: XNR_5809
SFI: SFUL_521
SALU: DC74_5960
SALL: SAZ_30880
STRE: GZL_02841
SLD: T261_1659
SLE: sle_24290(sle_24290)
SALJ: SMD11_3073
SEN: SACE_1242(cyp25)
 » show all
Taxonomy
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 (2005) 11599-607.
  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 (2005) 42188-97.
  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 (2007) 8725-33.
  Sequence
[sco:SCO6998]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.21.7
IUBMB Enzyme Nomenclature: 1.14.21.7
ExPASy - ENZYME nomenclature database: 1.14.21.7
BRENDA, the Enzyme Database: 1.14.21.7

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