BRENDA - Enzyme Database show
show all sequences of 1.14.14.156

CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime

Naur, P.; Hansen, C.; Bak, S.; Hansen, B.; Jensen, N.; Nielsen, H.; Halkier, B.; Arch. Biochem. Biophys. 409, 235-241 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli C43(DE3) cells, reconstitution of CYP79B1 monooxygenase requires a NADPH:cytochrome P450 reductase
Sinapis alba
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.029
-
L-tryptophan
at pH 7.6 and 30°C
Sinapis alba
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sinapis alba
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
713941
Sinapis alba
(E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
additional information
CYP79B1 is not able to metabolize L-phenylalanine or L-tyrosine
713941
Sinapis alba
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Sinapis alba
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
-
Sinapis alba
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Sinapis alba
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli C43(DE3) cells, reconstitution of CYP79B1 monooxygenase requires a NADPH:cytochrome P450 reductase
Sinapis alba
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Sinapis alba
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.029
-
L-tryptophan
at pH 7.6 and 30°C
Sinapis alba
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
713941
Sinapis alba
(E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
additional information
CYP79B1 is not able to metabolize L-phenylalanine or L-tyrosine
713941
Sinapis alba
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Sinapis alba
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
-
Sinapis alba
Other publictions for EC 1.14.14.156
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)
716536
Sanchez-Vallet
Tryptophan-derived secondary m ...
Arabidopsis thaliana
Plant J.
63
115-127
2010
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6
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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
1
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714117
Glawischnig
The role of cytochrome P450 en ...
Arabidopsis thaliana
Biochem. Soc. Trans.
34
1206-1208
2006
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1
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4
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1
1
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716733
Glawischnig
Camalexin is synthesized from ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
101
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2004
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3
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1
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1
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1
3
3
1
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713941
Naur
CYP79B1 from Sinapis alba conv ...
Sinapis alba
Arch. Biochem. Biophys.
409
235-241
2003
-
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1
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-
1
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5
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2
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1
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1
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1
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1
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2
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1
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1
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716592
Mikkelsen
Modulation of CYP79 genes and ...
Arabidopsis thaliana
Plant Physiol.
131
298-308
2003
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3
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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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2
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2
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715111
Zhao
Trp-dependent auxin biosynthes ...
Arabidopsis thaliana
Genes Dev.
16
3100-3112
2002
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3
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2
2
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715448
Mikkelsen
Cytochrome P450 CYP79B2 from A ...
Arabidopsis thaliana
J. Biol. Chem.
275
33712-33717
2000
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1
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6
1
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2
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4
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4
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1
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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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2
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4
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1
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1
1
1
1
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716797
Hull
Arabidopsis cytochrome P450s t ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
97
2379-2384
2000
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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
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