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thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
classical ping-pong mechanism
-
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
classical ping-pong mechanism
-
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
-
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
-
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
-
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
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
proposed catalytic mechanism of ketimine reductase
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
proposed catalytic mechanism of ketimine reductase
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
-
-
-
-
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1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
aminoethyl cysteine ketimine + NADPH + H+
thiomorpholine-3-carboxylate
-
-
-
?
cystathionine ketimine + NADH
cyclothionine + NAD+
cystathionine ketimine + NADPH
cyclothionine + NADP+
DELTA1-piperideine 2-carboxylate + NADH
? + NAD+
DELTA1-piperideine 2-carboxylate + NADPH
? + NADP+
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
glyocylate + methylamine + NADPH + H+
sarcosine + NADP+
-
-
-
?
lanthionine ketimine + NADH
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
lanthionine ketimine + NADPH
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
lanthionine ketimine + NADPH + H+
thiomorpholine-3,5-dicarboxylate
phenylpyruvate + methylamine + NADPH + H+
N-methyl-L-phenylalanine + NADP+
-
-
-
?
pyruvate + ethylamine + NADPH + H+
N-ethyl-L-alanine + NADP+
-
-
-
?
pyruvate + methylamine + NADPH + H+
N-methyl-L-alanine + NADP+
-
-
-
?
pyruvate + NH3 + NADPH + H+
L-alanine + NADP+
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
S-aminoethylcysteine ketimine + NADH
1,4-thiomorpholine 3-carboxylic acid + NAD+
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
thiomorpholine 3-carboxylate + NAD(P)+
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
additional information
?
-
cystathionine ketimine + NADH
cyclothionine + NAD+
-
-
-
-
?
cystathionine ketimine + NADH
cyclothionine + NAD+
-
-
-
ir
cystathionine ketimine + NADPH
cyclothionine + NADP+
-
-
-
-
?
cystathionine ketimine + NADPH
cyclothionine + NADP+
-
-
-
ir
DELTA1-piperideine 2-carboxylate + NADH
? + NAD+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADH
? + NAD+
-
-
-
-
ir
DELTA1-piperideine 2-carboxylate + NADPH
? + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH
? + NADP+
-
-
-
-
ir
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
-
?
lanthionine ketimine + NADH
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
-
-
-
-
?
lanthionine ketimine + NADH
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
-
-
-
ir
lanthionine ketimine + NADPH
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
-
-
-
-
?
lanthionine ketimine + NADPH
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
-
-
-
ir
lanthionine ketimine + NADPH + H+
thiomorpholine-3,5-dicarboxylate
-
-
-
?
lanthionine ketimine + NADPH + H+
thiomorpholine-3,5-dicarboxylate
low activity
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
S-aminoethylcysteine ketimine + NADH
1,4-thiomorpholine 3-carboxylic acid + NAD+
-
-
-
-
?
S-aminoethylcysteine ketimine + NADH
1,4-thiomorpholine 3-carboxylic acid + NAD+
-
-
L-enantiomer
ir
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
-
-
-
-
?
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
-
-
-
ir
thiomorpholine 3-carboxylate + NAD(P)+
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
-
-
-
?
thiomorpholine 3-carboxylate + NAD(P)+
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
-
-
?
additional information
?
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
additional information
?
-
purified recombinant human CRYM possesses substantial KR activity. Ketimine reductase is a typical imine reductase. Substrate specificity of recombinant human ketimine reductase (KR) toward DELTA1-piperideine-2-carboxylate (P2CR) and various noncyclized imine intermediates, overview. N-methyl-L-alanine is produced when human KR is incubated in the presence of methylamine, NADPH and pyruvate. Human KR catalyzes the reductive alkylamination of phenylpyruvate and glyoxylate in the presence of methylamine
-
-
-
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
-
-
?
additional information
?
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
additional information
?
-
purified recombinant human CRYM possesses substantial KR activity. Ketimine reductase is a typical imine reductase
-
-
-
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1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
aminoethyl cysteine ketimine + NADPH + H+
thiomorpholine-3-carboxylate
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
lanthionine ketimine + NADPH + H+
thiomorpholine-3,5-dicarboxylate
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
thiomorpholine 3-carboxylate + NAD(P)+
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
additional information
?
-
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
-
?
DELTA1-pyrrolidine 2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
-
?
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
-
-
-
-
?
thiomorpholine 3-carboxylate + NAD(P)+
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
-
-
-
?
thiomorpholine 3-carboxylate + NAD(P)+
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
-
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
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
-
-
?
additional information
?
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
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3,3',5'-L-triiodothyronine
3,5,3'-L-triiodothyronine
3,5-diiodothyronine
-
competitive inhibition
3,5-L-diiodothyronine
-
-
4,5-dibromopyrrole-2-carboxylate
DELTA1-piperideine 2-carboxylate
-
substrate inhibition
S-(2-aminoethyl)-L-cysteine ketimine
-
substrate inhibition
Triton X-100
-
irreversible inactivation
3,3',5'-L-triiodothyronine
-
competitive inhibition
3,3',5'-L-triiodothyronine
-
3,5,3'-L-triiodothyronine
-
competitive inhibition
3,5,3'-L-triiodothyronine
-
3,5,3'-triiodothyronine
-
the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3
3,5,3'-triiodothyronine
-
-
3,5,3'-triiodothyronine
-
the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3
3,5,3'-triiodothyronine
the enzyme shows strong binding to 3,5,3'-triiodothyronine (T3), the active form of thyroxine
3,5,3'-triiodothyronine
-
the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3
3,5,3'-triiodothyronine
-
the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3
3,5,3'-triiodothyronine
-
-
3,5,3'-triiodothyronine
-
the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3, especially at neutral pH, reversible inhibition
3,5,3'-triiodothyronine
-
the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3
3,5-diiodo-L-tyrosine
-
low competitive inhibition
4,5-dibromopyrrole-2-carboxylate
-
-
4,5-dibromopyrrole-2-carboxylate
-
-
4,5-dibromopyrrole-2-carboxylate
-
-
L-thyroxine
-
competitive inhibition
L-tyrosine
-
competitive inhibition
picolinate
-
-
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
pyrrole-2-carboxylate
-
-
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
pyrrole-2-carboxylate
-
-
additional information
-
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
-
additional information
the P2C reductase activity is potently inhibited by thyroid hormones, thyroid hormones and analogues docked into the active site of the crystal structure of human KR, overview
-
additional information
the P2C reductase activity is potently inhibited by thyroid hormones
-
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0.000035 - 0.035
3,3',5'-L-triiodothyronine
0.00075
3,5,3'-L-triiodothyronine
pH 7.2, 37°C, recombinant enzyme
0.000278
3,5,3'-triiodothyronine
-
with substrate S-(2-aminoethyl)-L-cysteine ketimine, pH 5.0, temperature not specified in the publication
0.313
3,5-diiodo-L-tyrosine
0.000032
3,5-diiodothyronine
-
pH 7.2, 37°C
0.032
3,5-L-diiodothyronine
pH 7.2, 37°C, recombinant enzyme
-
0.038
4,5-dibromopyrrole-2-carboxylate
-
pH 7.2, 37°C
1.8
DELTA1-piperideine 2-carboxylate
-
pH 7.2, 37°C
0.0006
L-thyroxine
pH 7.2, 37°C, recombinant enzyme
0.8
L-tyrosine
pH 7.2, 37°C, recombinant enzyme
1.7
S-(2-aminoethyl)-L-cysteine ketimine
-
pH 7.2, 37°C
0.000035
3,3',5'-L-triiodothyronine
-
pH 7.2, 37°C
0.035
3,3',5'-L-triiodothyronine
pH 7.2, 37°C, recombinant enzyme
0.313
3,5-diiodo-L-tyrosine
-
pH 7.2, 37°C
0.313
3,5-diiodo-L-tyrosine
pH 7.2, 37°C, recombinant enzyme
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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
evolution
enzymes that reduce DELTA1-pyrroline-5-carboxylate and DELTA1-piperideine-6-carboxylate are aldimine reductases whereas enzymes that reduce DELTA1-piperideine-2-carboxylate and DELTA1-pyrroline-2-carboxylate (P2C/Pyr2C) are ketimine reductases (KRs)
evolution
enzymes that reduce DELTA1-pyrroline-5-carboxylate and DELTA1-piperideine-6-carboxylate are aldimine reductases whereas enzymes that reduce DELTA1-piperideine-2-carboxylate and DELTA1-pyrroline-2-carboxylate (P2C/Pyr2C) are ketimine reductases (KRs)
malfunction
-
significance of CRYM/KR in psychiatric and neurological disease, overview
malfunction
-
Significance of CRYM/KR in psychiatric and neurological disease, overview. Two known point mutations of human CRYM, both of which are associated with nonsyndromic deafness
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
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
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
metabolism
-
the enzyme is involved in the pipecolate pathway, i.e. P2C reductase activity
metabolism
-
the enzyme is involved in the pipecolate pathway, i.e. P2C reductase activity
metabolism
-
the enzyme is involved in the pipecolate pathway, i.e. P2C reductase activity
metabolism
-
the enzyme is involved in the pipecolate pathway, i.e. P2C reductase activity
metabolism
-
the enzyme is involved in the pipecolate pathway, i.e. P2C reductase activity
metabolism
-
the enzyme is involved in the pipecolate pathway, i.e. P2C reductase activity
metabolism
lysine degradation may be divided into two distinct pathways, namely (1) the pipecolate pathway which involves oxidation at the alpha-amino position followed by reduction of the product (P2C) to pipecolate by ketimine reductase (KR), and (2) the saccharopine pathway which involves oxidation at the epsilon-amino position The saccharopine pathway is predominantly mitochondrial, whereas the pipecolate pathway is predominantly cytosolic (but with a portion occurring in the peroxisomes). The DELTA1-piperideine-2-carboxylate (P2C) reductase enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Unique presence of the pipecolate pathway in brain. Cerebral pipecolate pathway, overview
metabolism
lysine degradation may be divided into two distinct pathways, namely (1) the pipecolate pathway which involves oxidation at the alpha-amino position followed by reduction of the product (P2C) to pipecolate by ketimine reductase (KR), and (2) the saccharopine pathway which involves oxidation at the epsilon-amino position The saccharopine pathway is predominantly mitochondrial, whereas the pipecolate pathway is predominantly cytosolic (but with a portion occurring in the peroxisomes). The DELTA1-piperideine-2-carboxylate (P2C) reductase enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Unique presence of the pipecolate pathway in brain. Cerebral pipecolate pathway, overview
physiological function
-
mammalian thyroid hormone-binding protein CRYM has an additional biological role as a ketimine reductase, CRYM is a P2C reductase. CRYM shows an extremely strong affinity for 3,5,3'-triiodothyronine T3 in the presence of NADPH. The enzyme seems to be tightly regulated in vivo by 3,5,3'-triiodothyronine (T3) at low concentrations, T3 bioavailability is likely strongly dependent on the pipecolate pathway activity
physiological function
-
mammalian thyroid hormone-binding protein CRYM has an additional biological role as a ketimine reductase, CRYM is a P2C reductase. CRYM shows an extremely strong affinity for 3,5,3'-triiodothyronine T3 in the presence of NADPH. The enzyme seems to be tightly regulated in vivo by 3,5,3'-triiodothyronine (T3) at low concentrations, T3 bioavailability is likely strongly dependent on the pipecolate pathway activity
physiological function
-
mammalian thyroid hormone-binding protein CRYM has an additional biological role as a ketimine reductase, CRYM is a P2C reductase. CRYM shows an extremely strong affinity for 3,5,3'-triiodothyronine T3 in the presence of NADPH. The enzyme seems to be tightly regulated in vivo by 3,5,3'-triiodothyronine (T3) at low concentrations, T3 bioavailability is likely strongly dependent on the pipecolate pathway activity
physiological function
-
mammalian thyroid hormone-binding protein CRYM has an additional biological role as a ketimine reductase, CRYM is a P2C reductase. CRYM shows an extremely strong affinity for 3,5,3'-triiodothyronine T3 in the presence of NADPH. The enzyme seems to be tightly regulated in vivo by 3,5,3'-triiodothyronine (T3) at low concentrations, T3 bioavailability is likely strongly dependent on the pipecolate pathway activity. Levels of CRYM/KR substrates are important determinants in hearing as CRYM mRNA is highly expressed in human inner ear
physiological function
-
mammalian thyroid hormone-binding protein CRYM has an additional biological role as a ketimine reductase, CRYM is a P2C reductase. CRYM shows an extremely strong affinity for 3,5,3'-triiodothyronine T3 in the presence of NADPH. The enzyme seems to be tightly regulated in vivo by 3,5,3'-triiodothyronine (T3) at low concentrations, T3 bioavailability is likely strongly dependent on the pipecolate pathway activity. Possible involvement of CRYM in the development of mouse hair follicles during the anagen phase. Enzyme substrates (e.g. sulfur-containing cyclic ketimines such as S-(2-aminoethyl)-L-cysteine ketimine) may play a role in regulating cell growth and/or cell differentiation
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
physiological function
-
the thyroid hormone-binding protein CRYM has an additional biological role as a ketimine reductase, CRYM is a P2C reductase. CRYM shows an extremely strong affinity for 3,5,3'-triiodothyronine T3 in the presence of NADPH. The enzyme seems to be tightly regulated in vivo by 3,5,3'-triiodothyronine (T3) at low concentrations, T3 bioavailability is likely strongly dependent on the pipecolate pathway activity
physiological function
identification of ketimine reductase (KR) as mu-crystalin (CRYM)/cytosolic thyroid hormone binding protein (THBP). CRYM is a major mammalian THBP, which has the ability to strongly bind thyroid hormones in an NADPH-dependent fashion. It is also active as a DELTA1-piperideine-2-carboxylate (P2C) reductase, which catalyzes the NAD(P)H-dependent reduction of -C=N- (imine) double bonds of a number of cyclic ketimine substrates including sulfur-containing cyclic ketimines. P2C exists in equilibrium with its open-chain form under acidic conditions, but at neutral pH, P2C exists predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form). P2C can also exist as an enamine, but only at basic pH values. The enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Although KR is important in the formation of L-pipecolate in the brain, it is also an important source of L-proline. This proline (via proline oxidase) in turn is an important source of DELTA1-pyrroline-5-carboxylate (Pyr5C) and hence of glutamate and to a lesser extent ornithine. Ketimine reductase is involved in several diseases
physiological function
identification of ketimine reductase (KR) as mu-crystalin (CRYM)/cytosolic thyroid hormone binding protein (THBP). CRYM is a major mammalian THBP, which has the ability to strongly bind thyroid hormones in an NADPH-dependent fashion. It is also active as a DELTA1-piperideine-2-carboxylate (P2C) reductase, which catalyzes the NAD(P)H-dependent reduction of -C=N- (imine) double bonds of a number of cyclic ketimine substrates including sulfur-containing cyclic ketimines. P2C exists in equilibrium with its open-chain form under acidic conditions, but at neutral pH, P2C exists predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form). P2C can also exist as an enamine, but only at basic pH values. The enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Although KR is important in the formation of L-pipecolate in the brain, it is also an important source of L-proline. This proline (via proline oxidase) in turn is an important source of DELTA1-pyrroline-5-carboxylate (Pyr5C) and hence of glutamate and to a lesser extent ornithine. Ketimine reductase is involved in several diseases
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Nardini, M.; Ricci, G.; Caccuri, A.M.; Solinas, S.P.; Vesci, L.; Cavallini, D.
Purification and characterization of a ketimine-reducing enzyme
Eur. J. Biochem.
173
689-694
1988
Sus scrofa
brenda
Nardini, M.; Ricci, G.; Vesci, L.; Pecci, L.; Cavallini, D.
Bovine brain ketimine reductase
Biochim. Biophys. Acta
957
286-292
1988
Bos taurus
brenda
Hallen, A.; Jamie, J.F.; Cooper, A.J.
Lysine metabolism in mammalian brain an update on the importance of recent discoveries
Amino Acids
45
1249-1272
2013
Bos taurus, Homo sapiens, Macropus giganteus, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Hallen, A.; Cooper, A.J.; Smith, J.R.; Jamie, J.F.; Karuso, P.
Ketimine reductase/CRYM catalyzes reductive alkylamination of alpha-keto acids, confirming its function as an imine reductase
Amino Acids
47
2457-2461
2015
Homo sapiens (Q14894)
brenda
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
Neurochem. Res.
40
1252-1266
2015
Bos taurus, Homo sapiens, Mus musculus
brenda
Hallen, A.; Cooper, A.J.
Reciprocal control of thyroid binding and the pipecolate pathway in the brain
Neurochem. Res.
42
217-243
2017
Mus musculus (O54983), Homo sapiens (Q14894)
brenda