BRENDA - Enzyme Database

Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer

Zhao, B.; Guengerich, F.P.; Voehler, M.; Waterman, M.R.; J. Biol. Chem. 280, 42188-42197 (2005)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
1.14.19.69
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
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.14.19.69
Streptomyces coelicolor
-
isoform CYP158A2
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.19.69
2-hydroxy-1,4-naphthoquinone + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
-
687501
Streptomyces coelicolor
? + oxidized ferredoxin [iron-sulfur] cluster + H2O
about 70fold lower activity than with flaviolin
-
-
?
1.14.19.69
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
-
687501
Streptomyces coelicolor
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
?
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.14.19.69
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
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.19.69
2-hydroxy-1,4-naphthoquinone + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
-
687501
Streptomyces coelicolor
? + oxidized ferredoxin [iron-sulfur] cluster + H2O
about 70fold lower activity than with flaviolin
-
-
?
1.14.19.69
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
-
687501
Streptomyces coelicolor
3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
?