BRENDA - Enzyme Database show
show all sequences of 1.14.14.66

Elicitor-induced biosynthesis of psoralens in Ammi majus L. suspension cultures. Microsomal conversion of demethylsuberosin into (+)marmesin and psoralen

Hamerski, D.; Matern, U.; Eur. J. Biochem. 171, 369-375 (1988)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0103
-
demethylsuberosin
pH 7.5, 20°C
Ammi majus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Ammi majus
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ammi majus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Ammi majus
-
Storage Stability
Storage Stability
Organism
-70°C, stable for at least 6 months
Ammi majus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
demethylsuberosin + [reduced NADPH-hemoprotein reductase] + O2
-
744830
Ammi majus
(+)-marmesin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
-
Ammi majus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
-
80% of maximum activity
Ammi majus
25
-
95% of maximum activity
Ammi majus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
broad
Ammi majus
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Ammi majus
additional information
NADPH-hemoprotein reductase does not accept NADH
Ammi majus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Ammi majus
additional information
NADPH-hemoprotein reductase does not accept NADH
Ammi majus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0103
-
demethylsuberosin
pH 7.5, 20°C
Ammi majus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Ammi majus
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Ammi majus
-
Storage Stability (protein specific)
Storage Stability
Organism
-70°C, stable for at least 6 months
Ammi majus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
demethylsuberosin + [reduced NADPH-hemoprotein reductase] + O2
-
744830
Ammi majus
(+)-marmesin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
-
Ammi majus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
-
80% of maximum activity
Ammi majus
25
-
95% of maximum activity
Ammi majus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
broad
Ammi majus
Expression
Organism
Commentary
Expression
Ammi majus
expression is induced in response to treatment with elicitor preparations from either Alternaria carthami Chowdhury or Phytophthora megasperma f.sp. glycinea
up
Expression (protein specific)
Organism
Commentary
Expression
Ammi majus
expression is induced in response to treatment with elicitor preparations from either Alternaria carthami Chowdhury or Phytophthora megasperma f.sp. glycinea
up
Other publictions for EC 1.14.14.66
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)
744830
Hamerski
Elicitor-induced biosynthesis ...
Ammi majus
Eur. J. Biochem.
171
369-375
1988
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