HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.14.21.7 - biflaviolin synthase
Word Map on EC 1.14.21.7
- 1.14.21.7
- coelicolor
- heme
-
monooxygenases
-
hydrogen-bonded
-
regiospecificity
-
polymerize
-
polyketide
- phenol
-
ligand-free
-
bulkier
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Streptomyces coelicolor
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.14.21.7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
biflaviolin synthase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 flaviolin + NADPH + H+ + O2 = 3,3'-biflaviolin + NADP+ + 2 H2O
-
-
-
-
2 flaviolin + NADPH + H+ + O2 = 3,8'-biflaviolin + NADP+ + 2 H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxy-1,4-naphthoquinone + NADPH + H+ + O2
? + NADP+ + H2O
-
-
about 70fold lower activity than with flaviolin
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
-
-
-
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
-
-
plus some further biflaviolin isomer and some triflaviolin
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
-
-
with isoform CYP158A1, product 3,8'-biflaviolin is about 40% of total product. Isoform CYP158A1 generates a further biflaviolin isomer and some triflaviolin
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
-
-
plus some further biflaviolin isomer and some triflaviolin
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
Q9FCA6, Q9KZF5
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
Q9FCA6, Q9KZF5
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
Q9FCA6, Q9KZF5
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
flaviolin + NADPH + H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + NADP+ + H2O
Q9FCA6, Q9KZF5
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-phenylimidazole
-
crystallization data. Presence of malonic acid affects binding behaviour and increases inhibitory potency up to 2fold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0073
flaviolin
wild type isoform CYP158A2, at pH 8.2 and 37°C
0.0105
flaviolin
wild type isoform CYP158A1, at pH 8.2 and 37°C
0.0169
flaviolin
mutant K90I of isoform CYP158A1, at pH 8.2 and 37°C
0.0432
flaviolin
mutant I87K of isoform CYP158A2, at pH 8.2 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) pLysS cells; expressed in Escherichia coli BL21 (DE3) pLysS cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.21.7)
html completed
Information
