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Literature summary for 1.5.1.25 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

Inhibitors Comment Organism Structure
3,3',5'-L-triiodothyronine competitive inhibition Homo sapiens
3,5,3'-L-triiodothyronine competitive inhibition Homo sapiens
3,5,3'-triiodothyronine
-
Bos taurus
3,5,3'-triiodothyronine
-
Mus musculus
3,5-diiodo-L-tyrosine low competitive inhibition Homo sapiens
3,5-diiodothyronine competitive inhibition Homo sapiens
4,5-dibromopyrrole-2-carboxylate
-
Bos taurus
4,5-dibromopyrrole-2-carboxylate
-
Homo sapiens
4,5-dibromopyrrole-2-carboxylate
-
Mus musculus
DELTA1-piperideine 2-carboxylate substrate inhibition Homo sapiens
L-thyroxine competitive inhibition Homo sapiens
L-tyrosine competitive inhibition Homo sapiens
additional information in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview Homo sapiens
picolinate
-
Bos taurus
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
picolinate
-
Mus musculus
pyrrole-2-carboxylate
-
Bos taurus
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
pyrrole-2-carboxylate
-
Mus musculus
S-(2-aminoethyl)-L-cysteine ketimine substrate inhibition Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Homo sapiens
0.013
-
DELTA1-piperideine 2-carboxylate pH 7.2, 37°C Homo sapiens
0.021
-
DELTA2-thiazoline-2-carboxylate pH 7.2, 37°C Homo sapiens
0.028
-
S-(2-aminoethyl)-L-cysteine ketimine pH 7.2, 37°C Homo sapiens
0.045
-
DELTA1-pyrrolidine 2-carboxylate pH 7.2, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Mus musculus 5829
-
cytosol
-
Homo sapiens 5829
-
cytosol
-
Bos taurus 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DELTA1-piperideine 2-carboxylate + NADPH + H+ Mus musculus
-
L-pipecolate + NADP+
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+ Homo sapiens
-
L-pipecolate + NADP+
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+ Bos taurus
-
L-pipecolate + NADP+
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+ Mus musculus
-
L-proline + NADP+
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+ Homo sapiens
-
L-proline + NADP+
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+ Bos taurus
-
L-proline + NADP+
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+ Mus musculus
-
? + NADP+
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+ Homo sapiens
-
? + NADP+
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+ Bos taurus
-
? + NADP+
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+ Mus musculus
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+ Homo sapiens
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+ Bos taurus
-
1,4-thiomorpholine-3-carboxylate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Mus musculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
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
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

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
brain
-
Homo sapiens
-
brain
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
Mus musculus L-pipecolate + NADP+
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
Homo sapiens L-pipecolate + NADP+
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
-
Bos taurus L-pipecolate + NADP+
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
Mus musculus L-proline + NADP+
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
Homo sapiens L-proline + NADP+
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
-
Bos taurus L-proline + NADP+
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
Mus musculus ? + NADP+
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
Homo sapiens ? + NADP+
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
-
Bos taurus ? + NADP+
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
additional information in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview Homo sapiens ?
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
Mus musculus 1,4-thiomorpholine-3-carboxylate + NADP+
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
Homo sapiens 1,4-thiomorpholine-3-carboxylate + NADP+
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
-
Bos taurus 1,4-thiomorpholine-3-carboxylate + NADP+
-
?

Synonyms

Synonyms Comment Organism
CRYM
-
Mus musculus
CRYM
-
Homo sapiens
CRYM
-
Bos taurus
ketimine reductase
-
Mus musculus
ketimine reductase
-
Homo sapiens
ketimine reductase
-
Bos taurus
mu-crystallin
-
Mus musculus
mu-crystallin
-
Homo sapiens
mu-crystallin
-
Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.2
-
S-(2-aminoethyl)-L-cysteine ketimine pH 7.2, 37°C Homo sapiens
1.7
-
DELTA2-thiazoline-2-carboxylate pH 7.2, 37°C Homo sapiens
4.4
-
DELTA1-piperideine 2-carboxylate pH 7.2, 37°C Homo sapiens
6.6
-
DELTA1-pyrrolidine 2-carboxylate pH 7.2, 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
reduction reaction of S-(2-aminoethyl)-L-cysteine ketimine Mus musculus
7.2
-
substrate reduction reaction Homo sapiens
7.2
-
substrate reduction reaction Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Mus musculus
NADPH
-
Homo sapiens
NADPH
-
Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000032
-
3,5-diiodothyronine pH 7.2, 37°C Homo sapiens
0.000035
-
3,3',5'-L-triiodothyronine pH 7.2, 37°C Homo sapiens
0.038
-
4,5-dibromopyrrole-2-carboxylate pH 7.2, 37°C Homo sapiens
0.313
-
3,5-diiodo-L-tyrosine pH 7.2, 37°C Homo sapiens
1.7
-
S-(2-aminoethyl)-L-cysteine ketimine pH 7.2, 37°C Homo sapiens
1.8
-
DELTA1-piperideine 2-carboxylate pH 7.2, 37°C Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0027
-
pH 7.2, 37°C Homo sapiens pyrrole-2-carboxylate

General Information

General Information Comment Organism
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
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
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
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]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
7
-
S-(2-aminoethyl)-L-cysteine ketimine pH 7.2, temperature 37°C Homo sapiens
80
-
DELTA2-thiazoline-2-carboxylate pH 7.2, 37°C Homo sapiens
148
-
DELTA1-pyrrolidine 2-carboxylate pH 7.2, 37°C Homo sapiens
339
-
DELTA1-piperideine 2-carboxylate pH 7.2, 37°C Homo sapiens