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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, ketimine reductase, ketimine-reducing enzyme, mu-crystallin, P2C reductase, reductase, ketimine, Thyroid hormone-binding protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CRYM
ketimine reductase
ketimine-reducing enzyme
-
-
-
-
mu-crystallin
P2C reductase
reductase, ketimine
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-
-
-
Thyroid hormone-binding protein
ketimine reductase
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-
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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+
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
-
-
-
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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
phenylpyruvate + methylamine + NADPH + H+
N-methyl-L-phenylalanine + NADP+
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + 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+
-
-
-
-
?
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
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+
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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+
-
-
-
-
?
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
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-
-
ir
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
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-
?
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
?
-
-
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
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-
?
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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
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + 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+
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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+
-
-
-
-
?
S-(2-aminoethyl)-L-cysteine ketimine + NADPH + H+
1,4-thiomorpholine-3-carboxylate + 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
-
-
?
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 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
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-
?
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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
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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
NADPH
-
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview
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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
-
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
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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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000278
3,5,3'-triiodothyronine
-
with substrate S-(2-aminoethyl)-L-cysteine ketimine, pH 5.0, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
highly purified recombinantly expressed human CRYM possesses substantial ketimine reductase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
7.2
4.5
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reaction with S-aminoethylcysteine ketimine or lanthionine ketimine, acetate buffer or phosphate buffer
5
-
reaction with S-aminoethylcysteine ketimine and NADH, cystathionine ketimine and NADPH or 1-piperidine 2-carboxylate and NADPH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high enzyme expression level, expression of the CRYM transcript follows the hair growth cycle with a significant increase in expression during mid- and late anagen growth phases
brenda
additional information
-
CRYM/KR mRNA in the mouse is most highly expressed in skin among the tissues evaluated, followed by brain and heart
brenda
-
very low expression in cerebellum compared to cerebrum, high overall expression level
brenda
-
levels of thyroid hormone binding capacity for cytosolic NADPH-dependent T3 binding are noticeably lower in the cerebellum than in the cerebrum of adult rat brain at all stages of development. NADPH-dependent T3 binding is only detected in kidney, liver, heart and spleen after birth, increasing over the next 6 weeks. NADPH-dependent T3 binding is detected in cerebrum and cerebellum 5 days before birth, increasing with a sharp transient spike at the time of birth, that is specific for the brain, particularly in cerebrum, and cannot be seen in other tissues. The NADPH-dependent T3 binding in cerebrum decreases after birth, but begins to increase again 2 weeks after birth. The level in cerebellum does not show this increase. The brain may contain at least two distinct P2C reductases/ketimine reductase, one of which is predominant in the fore-brain and another that is prominent in the cerebellum
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
malfunction
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significance of CRYM/KR in psychiatric and neurological disease, overview
malfunction
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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
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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
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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
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
Show AA Sequence and Transmembrane Helices (843 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
irreversible inactivation at protein concentration below 1 mg/ml. Complete loss of activity after 24 h at 4°C. Higher protein concentrations or 10% glycerol prevent enzyme inactivation. 30% loss of activity aftter 7 days at 4°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
steroid hormones have a marked effect on the expression of CRYM, e.g. androgens induce CRYM expression in bovine mammary glands
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steroid hormones have a marked effect on the expression of CRYM, e.g. androgens induce CRYM expression in human prostate cancer
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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