EC Number | Inhibitors | Comment | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | 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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.5.1.25 | cytosol | - |
Mus musculus | 5829 | - |
1.5.1.25 | cytosol | - |
Homo sapiens | 5829 | - |
1.5.1.25 | cytosol | - |
Bos taurus | 5829 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.25 | Bos taurus | - |
- |
- |
1.5.1.25 | Homo sapiens | - |
- |
- |
1.5.1.25 | Mus musculus | - |
- |
- |
EC Number | Reaction | Comment | 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 | Mus musculus | |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.5.1.25 | brain | - |
Mus musculus | - |
1.5.1.25 | brain | - |
Homo sapiens | - |
1.5.1.25 | brain | - |
Bos taurus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | 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 | 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 | 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 | 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 | Homo sapiens | ? | - |
? | |
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+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.25 | CRYM | - |
Mus musculus |
1.5.1.25 | CRYM | - |
Homo sapiens |
1.5.1.25 | CRYM | - |
Bos taurus |
1.5.1.25 | ketimine reductase | - |
Mus musculus |
1.5.1.25 | ketimine reductase | - |
Homo sapiens |
1.5.1.25 | ketimine reductase | - |
Bos taurus |
1.5.1.25 | mu-crystallin | - |
Mus musculus |
1.5.1.25 | mu-crystallin | - |
Homo sapiens |
1.5.1.25 | mu-crystallin | - |
Bos taurus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.1.25 | 37 | - |
assay at | Homo sapiens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | 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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.1.25 | 7.2 | - |
reduction reaction of S-(2-aminoethyl)-L-cysteine ketimine | Mus musculus |
1.5.1.25 | 7.2 | - |
substrate reduction reaction | Homo sapiens |
1.5.1.25 | 7.2 | - |
substrate reduction reaction | Bos taurus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.25 | NADPH | - |
Mus musculus | |
1.5.1.25 | NADPH | - |
Homo sapiens | |
1.5.1.25 | NADPH | - |
Bos taurus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | 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 |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
1.5.1.25 | 0.0027 | - |
pH 7.2, 37°C | Homo sapiens | pyrrole-2-carboxylate |
EC Number | General Information | Comment | 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 | Mus musculus |
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 | 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 |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | 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 |