BRENDA - Enzyme Database
show all sequences of 1.14.19.69

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)
Crystallization
Organism
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces coelicolor
-
isoform CYP158A2
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
-
-
?
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)
Crystallization
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
-
-
?
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
-
-
-
?
Other publictions for EC 1.14.19.69
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
726807
Zhao
The role of Ile87 of CYP158A2 ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Arch. Biochem. Biophys.
518
127-132
2012
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1
1
2
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4
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4
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5
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1
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4
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2
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4
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4
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685184
Zhao
Different binding modes of two ...
Streptomyces coelicolor
Biochemistry
46
8725-8733
2007
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1
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3
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1
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1
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685076
Zhao
Ligand-assisted inhibition in ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Biochemistry
45
7493-7500
2006
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1
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1
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44
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687498
Zhao
Binding of two flaviolin subst ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
J. Biol. Chem.
280
11599-11607
2005
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-
1
1
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46
-
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1
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2
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1
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2
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1
2
1
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1
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2
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1
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687501
Zhao
Role of active site water mole ...
Streptomyces coelicolor
J. Biol. Chem.
280
42188-42197
2005
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1
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3
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2
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1
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2
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