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Literature summary extracted from

  • Hallen, A.; Cooper, A.J.; Jamie, J.F.; Karuso, P.
    Insights into enzyme catalysis and thyroid hormone regulation of cerebral ketimine reductase/mu-crystallin under physiological conditions (2015), Neurochem. Res., 40, 1252-1266 .
    View publication on PubMed

Inhibitors

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

KM Value [mM]

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

Localization

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
-

Natural Substrates/ Products (Substrates)

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+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.25 Bos taurus
-
-
-
1.5.1.25 Homo sapiens
-
-
-
1.5.1.25 Mus musculus
-
-
-

Reaction

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

Source Tissue

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
-

Substrates and Products (Substrate)

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+
-
?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment 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 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

pH Optimum

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

Cofactor

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

Ki Value [mM]

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

IC50 Value

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

General Information

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

kcat/KM [mM/s]

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