1.14.19.69: biflaviolin synthase

This is an abbreviated version!
For detailed information about biflaviolin synthase, go to the full flat file.

Reaction

2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ +

Synonyms

CYP 158A2, CYP158A1, CYP158A2, cytochrome P450 158A2, EC 1.14.21.7

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.19 With oxidation of a pair of donors resulting in the reduction of O₂ to two molecules of water

                1.14.19.69 biflaviolin synthase

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Results	in table
29	AA Sequence
2	Application
3	Cloned(Commentary)
2	Cofactor
5	Crystallization (Commentary)
1	Inhibitors
4	KM Value [mM]
4	Natural Substrates/ Products (Substrates)
104	Organism
1	Pathway
4	Protein Variants
2	Purification (Commentary)
2	Reaction
10	Reference
20	Substrates and Products (Substrate)
7	Synonyms
1	Systematic Name
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.19.69 - biflaviolin synthase

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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

Streptomyces coelicolor

-

687501

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

Streptomyces coelicolor

-

687498

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

Streptomyces coelicolor

-

685184

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

Streptomyces coelicolor

Q9FCA6, Q9KZF5

726807

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

Streptomyces coelicolor

-

685076