EC Number   |
General Information |
Reference |
|---|
    1.1.1.21 | evolution |
aldose reductase (AKR1B1) is a member of the aldo-keto reductase superfamily |
738833 |
| 1.1.1.21 | evolution |
aldose reductase (ALR2) is a member of aldo-keto reductase superfamily |
-, 738161 |
| 1.1.1.21 | evolution |
aldose reductase belongs to the aldoketo reductase superfamily, which includes several enzymes that catalyze oxidation and reduction reactions involved in various cellular processes |
-, 739113 |
| 1.1.1.21 | evolution |
human aldose reductase (AKR1B1) is a member of the aldo-keto reductase superfamily, which consists of 15 families, 3 of which are mammalian containing the thirteen human aldo-keto reductase enzymes currently identified |
738833 |
| 1.1.1.21 | evolution |
the enzyme AKR1B1 belongs to the AKR1B subfamily |
738031 |
| 1.1.1.21 | evolution |
the enzyme AKR1B10 belongs to the AKR1B subfamily |
738031 |
| 1.1.1.21 | evolution |
the enzyme belongs to the aldo-keto reductase superfamily |
739481 |
| 1.1.1.21 | malfunction |
aldose reductase inhibition prevents hypoxia-induced increase in hypoxia-inducible factor-1alpha and vascular endothelial growth factor by regulating 26 S proteasome-mediated protein degradation in colon cancer cells, molecular mechanism, overview. Inhibition of hypoxia-induced HIF-1 protein accumulation by enzyme inhibition is abolished in the presence of MG132, a potent inhibitor of the 26 S proteasome. Enzyme inhibition also prevents the hypoxia-induced inflammatory molecules such as Cox-2 and PGE2 and expression of extracellular matrix proteins such as MMP2, vimentin, uPAR, and lysyl oxidase 2, overview |
722714 |
| 1.1.1.21 | malfunction |
carnosine-propanals are converted to carnosine-propanols in the lysates of heart, skeletal muscle, and brain tissue from wild-type but not AR-null mice. In comparison with wild-type mice, the urinary excretion of carnosine-propanols is decreased in AR-null mice, overview |
738593 |
| 1.1.1.21 | malfunction |
enzyme deficiency-induced microglia/macrophages induce the M2 rather than the M1 response (classically activated pro-inflammatory (M1) or alternatively activated anti-inflammatory (M2) cells) and promote locomotion recovery after spinal cord injury in mice. In the in vitro experiments, microglia cell lines (N9 or BV2) are treated with the enzyme inhibitor fidarestat. Enzyme inhibition causes 4-hydroxynonenal accumulation, which induces the phosphorylation of the cAMP response element-binding. Enzyme deficiency causes NF-kappaB downregulation and CREB upregulation after spinal cord injury in mice |
-, 739113 |
