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Information on EC 1.5.1.25 - thiomorpholine-carboxylate dehydrogenase
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1.5.1.25 thiomorpholine-carboxylate dehydrogenaseIUBMB Comments
The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, but more slowly.
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Word Map
- 1.5.1.25
-
thyroid
-
nadph-dependent
-
bioavailability
- cerebral
-
unsaturated
-
ovine
- l-cystathionine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
CRYM, CtBP, cytosolic thyroid hormone binding protein, DELTA1-piperideine-2-carboxylate reductase, ketimine reductase, ketimine-reducing enzyme, KR/CRYM/CTBP, More, mu-crystallin, P2C reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CRYM
CtBP
cytosolic thyroid hormone binding protein
DELTA1-piperideine-2-carboxylate reductase
ketimine reductase
ketimine-reducing enzyme
-
-
-
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KR/CRYM/CTBP
mu-crystallin
P2C reductase
PLP-dependent amino acid gamma-substitution enzyme
PYCR2
Pyr2C reductase
reductase, ketimine
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-
-
-
THBP
thyroid hormone binding protein
Thyroid hormone-binding protein
additional information
ketimine reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
classical ping-pong mechanism
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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
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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
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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
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
-
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reduction
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
thiomorpholine-3-carboxylate:NAD(P)+ 5,6-oxidoreductase
The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
115232-54-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aminoethyl cysteine ketimine + NADPH + H+
thiomorpholine-3-carboxylate
-
-
-
?
phenylpyruvate + methylamine + NADPH + H+
N-methyl-L-phenylalanine + 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+
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+
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-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
lanthionine ketimine + NADH
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
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-
-
-
?
lanthionine ketimine + NADH
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
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-
-
ir
lanthionine ketimine + NADPH
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
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-
-
-
?
lanthionine ketimine + NADPH
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
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-
-
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+
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-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
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-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
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-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
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-
-
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?
S-aminoethylcysteine ketimine + NADH
1,4-thiomorpholine 3-carboxylic acid + NAD+
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-
-
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?
S-aminoethylcysteine ketimine + NADH
1,4-thiomorpholine 3-carboxylic acid + NAD+
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L-enantiomer
ir
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
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-
-
-
?
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
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-
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ir
thiomorpholine 3-carboxylate + NAD(P)+
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
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-
-
?
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
?
-
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
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-
?
additional information
?
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reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
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additional information
?
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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
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-
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additional information
?
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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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aminoethyl cysteine ketimine + NADPH + H+
thiomorpholine-3-carboxylate
-
-
-
?
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+
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+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + NADP+
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-
-
-
?
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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reduction rate for cystathionine ketimine, lanthionine ketimine and DELTA1-piperidine 2-carboxylate is higher with NADPH than with NADH. Reduction rate for S-aminoethylcysteine with NADH is higher than with NADPH
NADH
-
NADH and NADPH show equal activity with cystathionine ketimine as substrate. Reduction of lanthionine ketimine with NADPH is faster than reduction with NADH. Reduction of S-aminoethylcysteine with NADH is faster than reduction with NADPH
NADPH
-
reduction rate for cystathionine ketimine, lanthionine ketimine and DELTA1-piperidine 2-carboxylate is higher with NADPH than with NADH. Reduction rate for S-aminoethylcysteine with NADH is higher than with NADPH
NADPH
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NADH and NADPH show equal activity with cystathionine ketimine as substrate. Reduction of lanthionine ketimine with NADPH is faster than reduction with NADH. Reduction of S-aminoethylcysteine with NADH is faster than reduction with NADPH
additional information
the enzyme uses NADH and NADPH as reductant about equally well
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additional information
the enzyme uses NADH and NADPH as reductant about equally well
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5,3'-triiodothyronine
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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
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
-
the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3, especially at neutral pH, reversible inhibition
3,5,3'-triiodothyronine
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the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3
picolinate
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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
-
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
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.33
DELTA1-Piperidine 2-carboxylate
-
reaction with DELTA1-piperidine-2-carboxylate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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