1.5.1.25: thiomorpholine-carboxylate dehydrogenase
This is an abbreviated version!
For detailed information about thiomorpholine-carboxylate dehydrogenase, go to the full flat file.
Word Map on EC 1.5.1.25
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1.5.1.25
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thyroid
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nadph-dependent
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bioavailability
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cerebral
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unsaturated
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ovine
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l-cystathionine
- 1.5.1.25
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thyroid
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nadph-dependent
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bioavailability
- cerebral
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unsaturated
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ovine
- l-cystathionine
Reaction
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, PLP-dependent amino acid gamma-substitution enzyme, PYCR2, Pyr2C reductase, reductase, ketimine, THBP, thyroid hormone binding protein, Thyroid hormone-binding protein
ECTree
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General Information
General Information on EC 1.5.1.25 - thiomorpholine-carboxylate dehydrogenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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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
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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
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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. 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
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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. 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
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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
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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
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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
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
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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
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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
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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
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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
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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
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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
