BRENDA - Enzyme Database
show all sequences of 1.5.1.25

Ketimine reductase/CRYM catalyzes reductive alkylamination of alpha-keto acids, confirming its function as an imine reductase

Hallen, A.; Cooper, A.J.; Smith, J.R.; Jamie, J.F.; Karuso, P.; Amino Acids 47, 2457-2461 (2015)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
3,5,3'-triiodothyronine
the enzyme shows strong binding to 3,5,3'-triiodothyronine (T3), the active form of thyroxine
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q14894
-
-
Reaction
Reaction
Commentary
Organism
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
the enzyme binds 2-oxo acids, such as pyruvate, in solution, and catalyzes the formation of N-alkyl-amino acids from alkylamines and 2-oxo acids via reduction of imine intermediates. Mechanistically, ketimine reductase/CRYM acts as a classical imine reductase
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
741584
Homo sapiens
L-pipecolate + NADP+
-
-
-
?
glyocylate + methylamine + NADPH + H+
-
741584
Homo sapiens
sarcosine + NADP+
-
-
-
?
additional information
human ketimine reductase/CRYM can utilize alkylamines (such as methylamine and ethylamine) and 2-oxo acids (such as pyruvate and phenylpyruvate) as enzyme substrates. Analysis of reaction intermediates, overview. Mammalian ketimine reductase reaction is known to be enantiospecific and only the L-enantiomer product is formed in vivo. A ketimine reductase/CRYM-catalyzed reaction at neutral pH in the reverse direction is not determined
741584
Homo sapiens
?
-
-
-
-
phenylpyruvate + methylamine + NADPH + H+
-
741584
Homo sapiens
N-methyl-L-phenylalanine + NADP+
-
-
-
?
pyruvate + ethylamine + NADPH + H+
-
741584
Homo sapiens
N-ethyl-L-alanine + NADP+
-
-
-
?
pyruvate + methylamine + NADPH + H+
-
741584
Homo sapiens
N-methyl-L-alanine + NADP+
-
-
-
?
pyruvate + NH3 + NADPH + H+
-
741584
Homo sapiens
L-alanine + NADP+
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3,5,3'-triiodothyronine
the enzyme shows strong binding to 3,5,3'-triiodothyronine (T3), the active form of thyroxine
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
741584
Homo sapiens
L-pipecolate + NADP+
-
-
-
?
glyocylate + methylamine + NADPH + H+
-
741584
Homo sapiens
sarcosine + NADP+
-
-
-
?
additional information
human ketimine reductase/CRYM can utilize alkylamines (such as methylamine and ethylamine) and 2-oxo acids (such as pyruvate and phenylpyruvate) as enzyme substrates. Analysis of reaction intermediates, overview. Mammalian ketimine reductase reaction is known to be enantiospecific and only the L-enantiomer product is formed in vivo. A ketimine reductase/CRYM-catalyzed reaction at neutral pH in the reverse direction is not determined
741584
Homo sapiens
?
-
-
-
-
phenylpyruvate + methylamine + NADPH + H+
-
741584
Homo sapiens
N-methyl-L-phenylalanine + NADP+
-
-
-
?
pyruvate + ethylamine + NADPH + H+
-
741584
Homo sapiens
N-ethyl-L-alanine + NADP+
-
-
-
?
pyruvate + methylamine + NADPH + H+
-
741584
Homo sapiens
N-methyl-L-alanine + NADP+
-
-
-
?
pyruvate + NH3 + NADPH + H+
-
741584
Homo sapiens
L-alanine + NADP+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
physiological function
the enzyme is the main cytosolic thyroid hormone binding protein and shows strong binding to 3,5,3'-triiodothyronine (T3), the active form of thyroxine. Ketimine reductase/CRYM substrate levels and T3 bioavailability are reciprocally linked. Human ketimine reductase/CRYM catalyzes reduction of non-cyclic imines. Since a ketimine reductase/CRYM-catalyzed reaction at neutral pH in the reverse direction cannot be demonstrated, ketimine reductase/CRYM-catalyzed reductive amination/alkylamination of 2-oxo acids (or oxidation of L-amino acids/N-alkyl-L-amino acids) is not likely to be of physiological importance in mammals in vivo
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is the main cytosolic thyroid hormone binding protein and shows strong binding to 3,5,3'-triiodothyronine (T3), the active form of thyroxine. Ketimine reductase/CRYM substrate levels and T3 bioavailability are reciprocally linked. Human ketimine reductase/CRYM catalyzes reduction of non-cyclic imines. Since a ketimine reductase/CRYM-catalyzed reaction at neutral pH in the reverse direction cannot be demonstrated, ketimine reductase/CRYM-catalyzed reductive amination/alkylamination of 2-oxo acids (or oxidation of L-amino acids/N-alkyl-L-amino acids) is not likely to be of physiological importance in mammals in vivo
Homo sapiens
Other publictions for EC 1.5.1.25
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)
741584
Hallen
Ketimine reductase/CRYM catal ...
Homo sapiens
Amino Acids
47
2457-2461
2015
-
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1
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1
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1
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7
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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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7
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1
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1
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1
1
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743354
Hallen
Insights into enzyme catalysi ...
Bos taurus, Homo sapiens, Mus musculus
Neurochem. Res.
40
1252-1266
2015
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20
5
3
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-
15
-
3
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3
-
3
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16
-
1
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4
3
-
-
3
6
-
1
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-
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3
-
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1
20
6
5
3
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15
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3
-
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16
-
1
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4
3
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-
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4
4
-
4
4
741580
Hallen
Lysine metabolism in mammalia ...
Bos taurus, Homo sapiens, Macropus giganteus, Mus musculus, Rattus norvegicus, Sus scrofa
Amino Acids
45
1249-1272
2013
-
-
-
-
-
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6
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6
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9
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6
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4
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16
1
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9
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1
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6
1
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6
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6
1
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6
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9
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4
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16
1
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9
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1
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2
14
14
2
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440358
Nardini
Purification and characterizat ...
Sus scrofa
Eur. J. Biochem.
173
689-694
1988
-
-
-
-
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1
1
4
-
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2
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3
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1
1
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1
1
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8
-
-
-
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3
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2
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2
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1
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1
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4
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2
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1
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1
1
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8
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3
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440359
Nardini
Bovine brain ketimine reductas ...
Bos taurus
Biochim. Biophys. Acta
957
286-292
1988
-
-
-
-
-
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6
1
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2
-
-
1
-
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1
1
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1
1
1
8
1
-
-
-
-
2
-
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2
-
-
-
-
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-
2
-
-
-
-
-
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6
1
-
2
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-
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-
1
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1
1
1
8
1
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2
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