BRENDA - Enzyme Database

Insights into enzyme catalysis and thyroid hormone regulation of cerebral ketimine reductase/mu-crystallin under physiological conditions

Hallen, A.; Cooper, A.J.; Jamie, J.F.; Karuso, P.; Neurochem. Res. 40, 1252-1266 (2015)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.5.1.25
3,3',5'-L-triiodothyronine
competitive inhibition
Homo sapiens
1.5.1.25
3,5,3'-L-triiodothyronine
competitive inhibition
Homo sapiens
1.5.1.25
3,5,3'-triiodothyronine
-
Bos taurus
1.5.1.25
3,5,3'-triiodothyronine
-
Mus musculus
1.5.1.25
3,5-diiodo-L-tyrosine
low competitive inhibition
Homo sapiens
1.5.1.25
3,5-diiodothyronine
competitive inhibition
Homo sapiens
1.5.1.25
4,5-dibromopyrrole-2-carboxylate
-
Bos taurus
1.5.1.25
4,5-dibromopyrrole-2-carboxylate
-
Homo sapiens
1.5.1.25
4,5-dibromopyrrole-2-carboxylate
-
Mus musculus
1.5.1.25
DELTA1-piperideine 2-carboxylate
substrate inhibition
Homo sapiens
1.5.1.25
L-thyroxine
competitive inhibition
Homo sapiens
1.5.1.25
L-tyrosine
competitive inhibition
Homo sapiens
1.5.1.25
additional information
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
Homo sapiens
1.5.1.25
picolinate
-
Bos taurus
1.5.1.25
picolinate
; competitive inhibition, picolinate is a much poorer inhibitor than pyrrole-2-carboxylate because it does not possess a ring -NH and relies on a relatively weak ring interaction
Homo sapiens
1.5.1.25
picolinate
-
Mus musculus
1.5.1.25
pyrrole-2-carboxylate
-
Bos taurus
1.5.1.25
pyrrole-2-carboxylate
; competitive inhibition, pyrrole-2-carboxylate is an effective inhibitor of ketimine reductase/CRYM mainly as a result of the -NH hydrogen bonding to an active site residue
Homo sapiens
1.5.1.25
pyrrole-2-carboxylate
-
Mus musculus
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine
substrate inhibition
Homo sapiens
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5.1.25
additional information
-
additional information
Michaelis-Menten kinetics
Homo sapiens
1.5.1.25
0.013
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.021
-
DELTA2-thiazoline-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.028
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.045
-
DELTA1-pyrrolidine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.5.1.25
cytosol
-
Bos taurus
5829
-
1.5.1.25
cytosol
-
Homo sapiens
5829
-
1.5.1.25
cytosol
-
Mus musculus
5829
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
Mus musculus
-
L-pipecolate + NADP+
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
Homo sapiens
-
L-pipecolate + NADP+
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
Bos taurus
-
L-pipecolate + NADP+
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
Mus musculus
-
L-proline + NADP+
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
Homo sapiens
-
L-proline + NADP+
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
Bos taurus
-
L-proline + NADP+
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
Mus musculus
-
? + NADP+
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
Homo sapiens
-
? + NADP+
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
Bos taurus
-
? + NADP+
-
-
?
1.5.1.25
additional information
Homo sapiens
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
?
-
-
-
1.5.1.25
additional information
Bos taurus
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
?
-
-
-
1.5.1.25
additional information
Mus musculus
the non-sulfur substrates exist in equilibrium with openchain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
?
-
-
-
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
Mus musculus
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
Homo sapiens
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
Bos taurus
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.5.1.25
Bos taurus
-
-
-
1.5.1.25
Homo sapiens
-
-
-
1.5.1.25
Mus musculus
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
Reaction ID
1.5.1.25
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
in silico docking of various ligands into the active site of the X-ray structure of the enzyme suggests an unusual catalytic mechanism involving an arginine residue as a proton donor
Bos taurus
1.5.1.25
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
in silico docking of various ligands into the active site of the X-ray structure of the enzyme suggests an unusual catalytic mechanism involving an arginine residue as a proton donor, proposed mechanism for the reaction catalyzed by ketimine reductase/CRYM, overview
Homo sapiens
1.5.1.25
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
in silico docking of various ligands into the active site of the X-ray structure of the enzyme suggests an unusual catalytic mechanism involving an arginine residue as a proton donor
Mus musculus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.5.1.25
brain
-
Bos taurus
-
1.5.1.25
brain
-
Homo sapiens
-
1.5.1.25
brain
-
Mus musculus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
743354
Mus musculus
L-pipecolate + NADP+
-
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
743354
Homo sapiens
L-pipecolate + NADP+
-
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
743354
Bos taurus
L-pipecolate + NADP+
-
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
743354
Mus musculus
L-proline + NADP+
-
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
743354
Homo sapiens
L-proline + NADP+
-
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
743354
Bos taurus
L-proline + NADP+
-
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
743354
Mus musculus
? + NADP+
-
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
743354
Homo sapiens
? + NADP+
-
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
743354
Bos taurus
? + NADP+
-
-
-
?
1.5.1.25
additional information
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
743354
Homo sapiens
?
-
-
-
-
1.5.1.25
additional information
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
743354
Bos taurus
?
-
-
-
-
1.5.1.25
additional information
the non-sulfur substrates exist in equilibrium with openchain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
743354
Mus musculus
?
-
-
-
-
1.5.1.25
additional information
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
743354
Homo sapiens
?
-
-
-
-
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
743354
Mus musculus
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
743354
Homo sapiens
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
743354
Bos taurus
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
?
Synonyms
EC Number
Synonyms
Commentary
Organism
1.5.1.25
CRYM
-
Bos taurus
1.5.1.25
CRYM
-
Homo sapiens
1.5.1.25
CRYM
-
Mus musculus
1.5.1.25
ketimine reductase
-
Bos taurus
1.5.1.25
ketimine reductase
-
Homo sapiens
1.5.1.25
ketimine reductase
-
Mus musculus
1.5.1.25
mu-crystallin
-
Bos taurus
1.5.1.25
mu-crystallin
-
Homo sapiens
1.5.1.25
mu-crystallin
-
Mus musculus
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.1.25
37
-
assay at
Homo sapiens
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.5.1.25
0.2
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
1.7
-
DELTA2-thiazoline-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
4.4
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
6.6
-
DELTA1-pyrrolidine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.5.1.25
7.2
-
substrate reduction reaction
Bos taurus
1.5.1.25
7.2
-
substrate reduction reaction
Homo sapiens
1.5.1.25
7.2
-
reduction reaction of S-(2-aminoethyl)-L-cysteine ketimine
Mus musculus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.5.1.25
NADPH
-
Homo sapiens
1.5.1.25
NADPH
-
Bos taurus
1.5.1.25
NADPH
-
Mus musculus
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.5.1.25
0.000032
-
3,5-diiodothyronine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.000035
-
3,3',5'-L-triiodothyronine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.038
-
4,5-dibromopyrrole-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.313
-
3,5-diiodo-L-tyrosine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
1.7
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
1.8
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
IC50 Value
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
1.5.1.25
0.0027
-
pH 7.2, 37°C
Homo sapiens
pyrrole-2-carboxylate
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.5.1.25
NADPH
-
Bos taurus
1.5.1.25
NADPH
-
Homo sapiens
1.5.1.25
NADPH
-
Mus musculus
IC50 Value (protein specific)
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
1.5.1.25
0.0027
-
pH 7.2, 37°C
Homo sapiens
pyrrole-2-carboxylate
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.5.1.25
3,3',5'-L-triiodothyronine
competitive inhibition
Homo sapiens
1.5.1.25
3,5,3'-L-triiodothyronine
competitive inhibition
Homo sapiens
1.5.1.25
3,5,3'-triiodothyronine
-
Bos taurus
1.5.1.25
3,5,3'-triiodothyronine
-
Mus musculus
1.5.1.25
3,5-diiodo-L-tyrosine
low competitive inhibition
Homo sapiens
1.5.1.25
3,5-diiodothyronine
competitive inhibition
Homo sapiens
1.5.1.25
4,5-dibromopyrrole-2-carboxylate
-
Bos taurus
1.5.1.25
4,5-dibromopyrrole-2-carboxylate
-
Homo sapiens
1.5.1.25
4,5-dibromopyrrole-2-carboxylate
-
Mus musculus
1.5.1.25
DELTA1-piperideine 2-carboxylate
substrate inhibition
Homo sapiens
1.5.1.25
L-thyroxine
competitive inhibition
Homo sapiens
1.5.1.25
L-tyrosine
competitive inhibition
Homo sapiens
1.5.1.25
additional information
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
Homo sapiens
1.5.1.25
picolinate
-
Bos taurus
1.5.1.25
picolinate
; competitive inhibition, picolinate is a much poorer inhibitor than pyrrole-2-carboxylate because it does not possess a ring -NH and relies on a relatively weak ring interaction
Homo sapiens
1.5.1.25
picolinate
-
Mus musculus
1.5.1.25
pyrrole-2-carboxylate
-
Bos taurus
1.5.1.25
pyrrole-2-carboxylate
; competitive inhibition, pyrrole-2-carboxylate is an effective inhibitor of ketimine reductase/CRYM mainly as a result of the -NH hydrogen bonding to an active site residue
Homo sapiens
1.5.1.25
pyrrole-2-carboxylate
-
Mus musculus
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine
substrate inhibition
Homo sapiens
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.5.1.25
0.000032
-
3,5-diiodothyronine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.000035
-
3,3',5'-L-triiodothyronine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.038
-
4,5-dibromopyrrole-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.313
-
3,5-diiodo-L-tyrosine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
1.7
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
1.8
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5.1.25
additional information
-
additional information
Michaelis-Menten kinetics
Homo sapiens
1.5.1.25
0.013
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.021
-
DELTA2-thiazoline-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.028
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
0.045
-
DELTA1-pyrrolidine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.5.1.25
cytosol
-
Bos taurus
5829
-
1.5.1.25
cytosol
-
Homo sapiens
5829
-
1.5.1.25
cytosol
-
Mus musculus
5829
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
Mus musculus
-
L-pipecolate + NADP+
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
Homo sapiens
-
L-pipecolate + NADP+
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
Bos taurus
-
L-pipecolate + NADP+
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
Mus musculus
-
L-proline + NADP+
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
Homo sapiens
-
L-proline + NADP+
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
Bos taurus
-
L-proline + NADP+
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
Mus musculus
-
? + NADP+
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
Homo sapiens
-
? + NADP+
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
Bos taurus
-
? + NADP+
-
-
?
1.5.1.25
additional information
Homo sapiens
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
?
-
-
-
1.5.1.25
additional information
Bos taurus
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
?
-
-
-
1.5.1.25
additional information
Mus musculus
the non-sulfur substrates exist in equilibrium with openchain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
?
-
-
-
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
Mus musculus
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
Homo sapiens
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
Bos taurus
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.5.1.25
brain
-
Bos taurus
-
1.5.1.25
brain
-
Homo sapiens
-
1.5.1.25
brain
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
743354
Mus musculus
L-pipecolate + NADP+
-
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
743354
Homo sapiens
L-pipecolate + NADP+
-
-
-
?
1.5.1.25
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
743354
Bos taurus
L-pipecolate + NADP+
-
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
743354
Mus musculus
L-proline + NADP+
-
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
743354
Homo sapiens
L-proline + NADP+
-
-
-
?
1.5.1.25
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
743354
Bos taurus
L-proline + NADP+
-
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
743354
Mus musculus
? + NADP+
-
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
743354
Homo sapiens
? + NADP+
-
-
-
?
1.5.1.25
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
743354
Bos taurus
? + NADP+
-
-
-
?
1.5.1.25
additional information
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
743354
Homo sapiens
?
-
-
-
-
1.5.1.25
additional information
the non-sulfur substrates exist in equilibrium with open chain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
743354
Bos taurus
?
-
-
-
-
1.5.1.25
additional information
the non-sulfur substrates exist in equilibrium with openchain forms at low acidic pH. At neutral pH, they exist predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form), while sulfur-containing cyclic ketimine substrates exist predominantly as the enzymatically unfavorable enamine form (in which the ring double bond is in the C=C form) at neutral pH
743354
Mus musculus
?
-
-
-
-
1.5.1.25
additional information
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
743354
Homo sapiens
?
-
-
-
-
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
743354
Mus musculus
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
743354
Homo sapiens
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
?
1.5.1.25
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
743354
Bos taurus
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.1.25
37
-
assay at
Homo sapiens
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.5.1.25
0.2
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, 37°C
Homo sapiens
1.5.1.25
1.7
-
DELTA2-thiazoline-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
4.4
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
6.6
-
DELTA1-pyrrolidine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.5.1.25
7.2
-
substrate reduction reaction
Bos taurus
1.5.1.25
7.2
-
substrate reduction reaction
Homo sapiens
1.5.1.25
7.2
-
reduction reaction of S-(2-aminoethyl)-L-cysteine ketimine
Mus musculus
General Information
EC Number
General Information
Commentary
Organism
1.5.1.25
metabolism
lysine is catabolized in mammalian tissues by two main pathways: the saccharopine pathway and the pipecolate pathway. The pipecolate pathway is the main route for lysine catabolism in the adult brain, whereas the saccharopine pathway predominates in extracerebral tissues. Iimportance of the pipecolate pathway in brain metabolism. Lysine/ornithine catabolism and interconnected pathways in mammalian tissues, and metabolic pathways involving sulfur-containing cyclic ketimines, overview
Bos taurus
1.5.1.25
metabolism
lysine is catabolized in mammalian tissues by two main pathways: the saccharopine pathway and the pipecolate pathway. The pipecolate pathway is the main route for lysine catabolism in the adult brain, whereas the saccharopine pathway predominates in extracerebral tissues. Importance of the pipecolate pathway in brain metabolism. Lysine/ornithine catabolism and interconnected pathways in mammalian tissues, and metabolic pathways involving sulfur-containing cyclic ketimines, overview
Homo sapiens
1.5.1.25
metabolism
lysine is catabolized in mammalian tissues by two main pathways: the saccharopine pathway and the pipecolate pathway. The pipecolate pathway is the main route for lysine catabolism in the adult brain, whereas the saccharopine pathway predominates in extracerebral tissues. Importance of the pipecolate pathway in brain metabolism. Lysine/ornithine catabolism and interconnected pathways in mammalian tissues, and metabolic pathways involving sulfur-containing cyclic ketimines, overview
Mus musculus
1.5.1.25
additional information
in silico docking of various substrates and small inhibitors into the active site of the X-ray structures of mouse ketimine reductase/CRYM in order to better understand the enzyme catalytic mechanism
Mus musculus
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.5.1.25
metabolism
lysine is catabolized in mammalian tissues by two main pathways: the saccharopine pathway and the pipecolate pathway. The pipecolate pathway is the main route for lysine catabolism in the adult brain, whereas the saccharopine pathway predominates in extracerebral tissues. Iimportance of the pipecolate pathway in brain metabolism. Lysine/ornithine catabolism and interconnected pathways in mammalian tissues, and metabolic pathways involving sulfur-containing cyclic ketimines, overview
Bos taurus
1.5.1.25
metabolism
lysine is catabolized in mammalian tissues by two main pathways: the saccharopine pathway and the pipecolate pathway. The pipecolate pathway is the main route for lysine catabolism in the adult brain, whereas the saccharopine pathway predominates in extracerebral tissues. Importance of the pipecolate pathway in brain metabolism. Lysine/ornithine catabolism and interconnected pathways in mammalian tissues, and metabolic pathways involving sulfur-containing cyclic ketimines, overview
Homo sapiens
1.5.1.25
metabolism
lysine is catabolized in mammalian tissues by two main pathways: the saccharopine pathway and the pipecolate pathway. The pipecolate pathway is the main route for lysine catabolism in the adult brain, whereas the saccharopine pathway predominates in extracerebral tissues. Importance of the pipecolate pathway in brain metabolism. Lysine/ornithine catabolism and interconnected pathways in mammalian tissues, and metabolic pathways involving sulfur-containing cyclic ketimines, overview
Mus musculus
1.5.1.25
additional information
in silico docking of various substrates and small inhibitors into the active site of the X-ray structures of mouse ketimine reductase/CRYM in order to better understand the enzyme catalytic mechanism
Mus musculus
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.5.1.25
7
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, temperature 37°C
Homo sapiens
1.5.1.25
80
-
DELTA2-thiazoline-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
148
-
DELTA1-pyrrolidine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
339
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.5.1.25
7
-
S-(2-aminoethyl)-L-cysteine ketimine
pH 7.2, temperature 37°C
Homo sapiens
1.5.1.25
80
-
DELTA2-thiazoline-2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
148
-
DELTA1-pyrrolidine 2-carboxylate
pH 7.2, 37°C
Homo sapiens
1.5.1.25
339
-
DELTA1-piperideine 2-carboxylate
pH 7.2, 37°C
Homo sapiens