Information on EC 1.14.21.7 - biflaviolin synthase

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The expected taxonomic range for this enzyme is: Streptomyces coelicolor

EC NUMBER
COMMENTARY hide
1.14.21.7
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RECOMMENDED NAME
GeneOntology No.
biflaviolin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 flaviolin + NADPH + H+ + O2 = 3,3'-biflaviolin + NADP+ + 2 H2O
show the reaction diagram
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2 flaviolin + NADPH + H+ + O2 = 3,8'-biflaviolin + NADP+ + 2 H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
flaviolin dimer and mompain biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
flaviolin,NADPH:oxygen oxidoreductase
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxy-1,4-naphthoquinone + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
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about 70fold lower activity than with flaviolin
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?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-phenylimidazole
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crystallization data. Presence of malonic acid affects binding behaviour and increases inhibitory potency up to 2fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0073 - 0.0432
flaviolin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
flaviolin
Streptomyces coelicolor
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pH 7.5, 37C
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complex of ferric CYP158A2 with substrate analogue 2-hydroxy-1,4-naphthoquinone, 2.15 A resolution, and the flaviolin ferrous dioxygen-bound CYP158A2 complex, to 1.8 A resolution. In the ferrous dioxygen-bound flaviolin complex, the three water molecules in the ferric flaviolin complex still occupy the same positions and form hydrogen bonds to the distal dioxygen atom. A continuous hydrogen-bonded water network connecting the active site to the protein surface is proposed to participate in the proton-delivery cascade, leading to dioxygen bond scission
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free enzyme and in complex with flaviolin, diffration to 1.75 and 1.62 A resolution, respectively.Upon ligand binding, a major conformational change takes place that closes the entry into the active site, partly due to repositioning of the F and G helices. Presence of two molecules of flaviolin in the closed active site that form a quasi-planar three-molecule stack including the heme
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free isoform CYP158A1, in complex with imidazole and in complex with flaviolin. Comparison of structures with isoform CYP158A2. In isoform CYP158A1, only one flaviolin molecule is present close to the heme iron, and the second flaviolin molecule binds at the entrance of the putative substrate access channel on the protein distal surface 9 A away
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I87K mutant of isoform CYP158A2, hanging drop vapor diffusion method, using 0.1 M bis-Tris (pH 6.5), 1.2 M ammonium dihydrogen phosphate
in complex with inhibitor 4-phenylimidazole, crystallization in presence of malonic acid. Diffraction to 1.5 A resolution. Presence of malonic acid affects binding behaviour and increases inhibitory potency up to 2fold. Two molecules of malonate are found above the single inhibitor molecule in the active site, linked between the BC loop and beta 1-4/beta6-1 strands via hydrogen bond interactions to stabilize the conformational changes of the BC loop and beta strands that take place upon inhibitor binding. 4-Phenylimidazole can launch an extensive hydrogen-bonding network in the region of the F/G helices which may stabilize the conformational changes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity chromatography and S-Sepharose/Q-Sepharose column chromatography; Ni2+ affinity chromatography and S-Sepharose/Q-Sepharose column chromatography
recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) pLysS cells; expressed in Escherichia coli BL21 (DE3) pLysS cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I87K
mutant of isoform CYP158A2, the mutation significantly changes the ratios of the dimerization products converting CYP158A2 into a CYP158A1-like monooxygenase
K90I
mutant of isoform CYP158A1, the catalytic activity of the mutant does not change at all compared with the wild type enzyme
I87K
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mutant of isoform CYP158A2, the mutation significantly changes the ratios of the dimerization products converting CYP158A2 into a CYP158A1-like monooxygenase
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K90I
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mutant of isoform CYP158A1, the catalytic activity of the mutant does not change at all compared with the wild type enzyme
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