BRENDA - Enzyme Database show
show all sequences of 1.5.3.2

Specificity of rabbit kidney demethylase

Moritani, M.; Tung, T.C.; Fujii, S.; Mito, H.; Izumiya, N.; Kenmochi, K.; Hirohata, R.; J. Biol. Chem. 209, 485-492 (1954)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
not inhibited by 0.01 M benzoate, 0.01 M quinine HCl, 0.01 M atabrine, 0.01 M KCN
Oryctolagus cuniculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.262
-
alpha-N-methyl-L-tryptophan
-
Oryctolagus cuniculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oryctolagus cuniculus
-
-
-
Reaction
Reaction
Commentary
Organism
an N-methyl-L-amino acid + H2O + O2 = an L-amino acid + formaldehyde + H2O2
reaction mechanism
Oryctolagus cuniculus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-N-methyl-L-histidine + O2 + H2O
-
392426
Oryctolagus cuniculus
L-histidine + formaldehyde + H2O2
-
-
-
?
alpha-N-methyl-L-tryptophan + O2 + H2O
alpha-N-methyl-L-tryptophan is identical with L-abrine
392426
Oryctolagus cuniculus
L-tryptophan + formaldehyde + H2O2
-
392426
Oryctolagus cuniculus
?
additional information
more substrates, not with: N-dimethyl-L-amino acid, N-methyl-D-amino acid, L-amino acid, D-amino acid
392426
Oryctolagus cuniculus
?
-
-
-
-
N-methyl-L-amino acid + O2 + H2O
enzyme requires the presence of a free alpha-carboxyl group in the substrate molecule, substrates with aromatic or heterocyclic substituents are more readily oxidized, followed by aliphatic N-methylamino acids with long side chain, more slowly activity towards N-methyl derivatives of beta-hydroxy-amino acids and of basic and acidic amino acids with exception of histidin, very slow demethylation of phenylsarcosine
392426
Oryctolagus cuniculus
L-amino acid + formaldehyde + H2O2
-
392426
Oryctolagus cuniculus
?
N-methyl-L-norleucine + O2 + H2O
-
392426
Oryctolagus cuniculus
L-norleucine + formaldehyde + H2O2
-
392426
Oryctolagus cuniculus
?
N-methyl-L-phenylalanine + O2 + H2O
-
392426
Oryctolagus cuniculus
L-phenylalanine + formaldehyde + H2O2
-
-
-
?
N-methyl-L-tyrosine + O2 + H2O
N-methyl-DL-tyrosine is identical with surinamine
392426
Oryctolagus cuniculus
L-tyrosine + formaldehyde + H2O2
-
-
-
?
N-methyldihydroxyphenyl-DL-alanine + O2 + H2O
-
392426
Oryctolagus cuniculus
formaldehyde + dihydroxyphenyl-DL-alanine + H2O2
-
-
-
?
N-methylvanillyl-L-alanine + O2 + H2O
-
392426
Oryctolagus cuniculus
?
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Oryctolagus cuniculus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
as prosthetic group
Oryctolagus cuniculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
as prosthetic group
Oryctolagus cuniculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
not inhibited by 0.01 M benzoate, 0.01 M quinine HCl, 0.01 M atabrine, 0.01 M KCN
Oryctolagus cuniculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.262
-
alpha-N-methyl-L-tryptophan
-
Oryctolagus cuniculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-N-methyl-L-histidine + O2 + H2O
-
392426
Oryctolagus cuniculus
L-histidine + formaldehyde + H2O2
-
-
-
?
alpha-N-methyl-L-tryptophan + O2 + H2O
alpha-N-methyl-L-tryptophan is identical with L-abrine
392426
Oryctolagus cuniculus
L-tryptophan + formaldehyde + H2O2
-
392426
Oryctolagus cuniculus
?
additional information
more substrates, not with: N-dimethyl-L-amino acid, N-methyl-D-amino acid, L-amino acid, D-amino acid
392426
Oryctolagus cuniculus
?
-
-
-
-
N-methyl-L-amino acid + O2 + H2O
enzyme requires the presence of a free alpha-carboxyl group in the substrate molecule, substrates with aromatic or heterocyclic substituents are more readily oxidized, followed by aliphatic N-methylamino acids with long side chain, more slowly activity towards N-methyl derivatives of beta-hydroxy-amino acids and of basic and acidic amino acids with exception of histidin, very slow demethylation of phenylsarcosine
392426
Oryctolagus cuniculus
L-amino acid + formaldehyde + H2O2
-
392426
Oryctolagus cuniculus
?
N-methyl-L-norleucine + O2 + H2O
-
392426
Oryctolagus cuniculus
L-norleucine + formaldehyde + H2O2
-
392426
Oryctolagus cuniculus
?
N-methyl-L-phenylalanine + O2 + H2O
-
392426
Oryctolagus cuniculus
L-phenylalanine + formaldehyde + H2O2
-
-
-
?
N-methyl-L-tyrosine + O2 + H2O
N-methyl-DL-tyrosine is identical with surinamine
392426
Oryctolagus cuniculus
L-tyrosine + formaldehyde + H2O2
-
-
-
?
N-methyldihydroxyphenyl-DL-alanine + O2 + H2O
-
392426
Oryctolagus cuniculus
formaldehyde + dihydroxyphenyl-DL-alanine + H2O2
-
-
-
?
N-methylvanillyl-L-alanine + O2 + H2O
-
392426
Oryctolagus cuniculus
?
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Oryctolagus cuniculus
Other publictions for EC 1.5.3.2
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)
392426
Moritani
Specificity of rabbit kidney d ...
Oryctolagus cuniculus
J. Biol. Chem.
209
485-492
1954
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1
1
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9
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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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9
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1
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