EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.5.1.25 | thiomorpholine 3-carboxylate + NAD(P)+ |
- |
Mus musculus |
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+ |
- |
? |
| 1.5.1.25 | thiomorpholine 3-carboxylate + NAD(P)+ |
- |
Homo sapiens |
3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+ |
- |
? |
| 1.5.1.25 | more |
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 |
Homo sapiens |
? |
- |
? |
| 1.5.1.25 | more |
in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview |
Homo sapiens |
? |
- |
? |
| 1.5.1.25 | lanthionine ketimine + NADPH + H+ |
low activity |
Homo sapiens |
thiomorpholine-3,5-dicarboxylate |
- |
? |
| 1.5.1.25 | more |
purified recombinant human CRYM possesses substantial KR activity. Ketimine reductase is a typical imine reductase |
Mus musculus |
? |
- |
- |
| 1.5.1.25 | more |
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 |
Homo sapiens |
? |
- |
- |
| 1.5.1.25 | more |
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase |
Mus musculus |
? |
- |
- |
| 1.5.1.25 | more |
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase |
Homo sapiens |
? |
- |
- |
| 1.5.1.25 | more |
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 |
? |
- |
? |
