BRENDA - Enzyme Database show
show all sequences of 1.14.14.84

Cloning and expression of a member of a new cytochrome P-450 family: Cytochrome P-450lin (CYP111) from Pseudomonas incognita

Ropp, J.; Gunsalus, I.; Sligar, S.; J. Bacteriol. 175, 6028-6037 (1993)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene linC, DNA and amino acid sequence determination and analysis, constitutive functional expression in Escherichia coli from plasmid pUC18 under control of the lac promoter
Pseudomonas putida
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
heme-containing cytochrome P450 enzyme
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
Pseudomonas putida
-
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
Pseudomonas putida PpG777
-
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
Q59723
a D110R strain, gene linC
-
Pseudomonas putida PpG777
Q59723
a D110R strain, gene linC
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli by anion exchange chromatography, ammonium sulfate fractionation, gel filtration, and a second step of anion exchange chromatography
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
717712
Pseudomonas putida
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
-
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
717712
Pseudomonas putida PpG777
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Pseudomonas putida
heme
-
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
gene linC, DNA and amino acid sequence determination and analysis, constitutive functional expression in Escherichia coli from plasmid pUC18 under control of the lac promoter
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Pseudomonas putida
heme
-
Pseudomonas putida
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
heme-containing cytochrome P450 enzyme
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
Pseudomonas putida
-
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
Pseudomonas putida PpG777
-
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli by anion exchange chromatography, ammonium sulfate fractionation, gel filtration, and a second step of anion exchange chromatography
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
717712
Pseudomonas putida
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
-
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
717712
Pseudomonas putida PpG777
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
-
-
?
General Information
General Information
Commentary
Organism
evolution
P45O1in is a member of the CYPIll P-450 monooxygenase gene family
Pseudomonas putida
metabolism
P-4501in catalyzes the 8-methyl hydroxylation of linalool as the first committed step of its utilization by Pseudomonas putida as the sole carbon source
Pseudomonas putida
additional information
P-4501in exhibits conservation in the axial cysteine heme ligand-containing peptide and the threonine region postulated to form an 02-binding pocket
Pseudomonas putida
General Information (protein specific)
General Information
Commentary
Organism
evolution
P45O1in is a member of the CYPIll P-450 monooxygenase gene family
Pseudomonas putida
metabolism
P-4501in catalyzes the 8-methyl hydroxylation of linalool as the first committed step of its utilization by Pseudomonas putida as the sole carbon source
Pseudomonas putida
additional information
P-4501in exhibits conservation in the axial cysteine heme ligand-containing peptide and the threonine region postulated to form an 02-binding pocket
Pseudomonas putida
Other publictions for EC 1.14.14.84
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)
701873
Bell
A cytochrome P450 class I elec ...
Novosphingobium aromaticivorans, Novosphingobium aromaticivorans ATCC 700278D-5
Appl. Microbiol. Biotechnol.
86
163-175
2010
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1
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1
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1
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1
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1
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1
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3
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1
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1
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1
1
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-
717712
Ropp
Cloning and expression of a me ...
Pseudomonas putida, Pseudomonas putida PpG777
J. Bacteriol.
175
6028-6037
1993
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1
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1
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2
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1
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2
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2
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1
2
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1
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2
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1
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2
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3
3
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-
390114
Bernhardt
Reconstitution of cytochrome P ...
Pseudomonas putida
Biochem. Biophys. Res. Commun.
187
310-317
1992
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1
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390113
Ullah
Protein components of a cytoch ...
Pseudomonas putida, Pseudomonas putida PpG777
J. Biol. Chem.
265
1345-1351
1990
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1
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1
1
4
4
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3
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1
1
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1
2
2
13
2
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3
1
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3
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1
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3
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1
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1
1
4
4
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1
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1
2
2
13
2
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3
1
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1
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2
2
-
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390112
Bhattacharyya
-
Chemical probes into the activ ...
Pseudomonas putida, Pseudomonas putida PpG777
Proc. Indian Acad. Sci. Chem. Sci.
93
1289-1304
1984
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3
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6
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1
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1
1
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6
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1
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1
1
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