EC Number   |
General Information |
Reference |
|---|
   1.5.1.25 | 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 |
741580 |
| 1.5.1.25 | 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 |
741580 |
| 1.5.1.25 | 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 |
741584 |
| 1.5.1.25 | 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 |
741580 |
