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1,6-dihydroxynaphthalene + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
1-naphtyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
2,3-dihydroxynaphthalene + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
2,6-dimethoxyphenol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
2-hydroxy-1,4-naphthoquinone + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
? + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
about 70fold lower activity than with flaviolin
-
?
2-naphtyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
3,5-dihydroxynaphthalene-2-carboxylic acid + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
1,6-dihydroxynaphthalene + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
1,6-dihydroxynaphthalene + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
1-naphtyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
1-naphtyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
2,3-dihydroxynaphthalene + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
2,3-dihydroxynaphthalene + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
2,6-dimethoxyphenol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
2,6-dimethoxyphenol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
2-naphtyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
2-naphtyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
plus some further biflaviolin isomer and some triflaviolin
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
with isoform CYP158A1, product 3,8'-biflaviolin is about 40% of total product. Isoform CYP158A1 generates a further biflaviolin isomer and some triflaviolin
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
plus some further biflaviolin isomer and some triflaviolin
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
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4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
CYP158A2 produces three isomers of biflaviolin and one triflaviolin
-
-
?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
isoform CYP158A1 can only produce 3,3'-biflaviolin and 3,8'-biflaviolin with quite different molar ratios compared with the products from CYP158A2
-
-
?
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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
-
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Zhao, B.; Waterman, M.R.; Isin, E.M.; Sundaramoorthy, M.; Podust, L.M.
Ligand-assisted inhibition in cytochrome P450 158A2 from Streptomyces coelicolor A3(2)
Biochemistry
45
7493-7500
2006
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Zhao, B.; Lamb, D.C.; Lei, L.; Kelly, S.L.; Yuan, H.; Hachey, D.L.; Waterman, M.R.
Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2
Biochemistry
46
8725-8733
2007
Streptomyces coelicolor
brenda
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.; 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
11599-11607
2005
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Zhao, B.; Guengerich, F.P.; Voehler, M.; 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
42188-42197
2005
Streptomyces coelicolor
brenda
Zhao, B.; Bellamine, A.; Lei, L.; Waterman, M.
The role of Ile87 of CYP158A2 in oxidative coupling reaction
Arch. Biochem. Biophys.
518
127-132
2012
Streptomyces coelicolor (Q9FCA6), Streptomyces coelicolor (Q9KZF5), Streptomyces coelicolor A3(2) (Q9FCA6), Streptomyces coelicolor A3(2) (Q9KZF5), Streptomyces coelicolor A3(2)
brenda
Okazawa, A.; Yamanishi, K.; Katsuyama, N.; Kitazawa, S.; Ogawa, T.; Ohta, D.
Identification of novel cytochrome P450 monooxygenases from actinomycetes capable of intermolecular oxidative C-C coupling reactions
J. Biosci. Bioeng.
129
23-30
2020
Streptomyces violaceusniger (G2P5C2), Streptomyces violaceusniger, Streptomyces violaceusniger Tu 4113 (G2P5C2)
brenda