EC Number   |
General Information |
Reference |
|---|
    1.1.1.2 | metabolism |
ALR2 is the first rate-determining enzyme in the polyol pathway and catalyzes the reduction of glucose to sorbitol in the presence of NADPH as a cofactor. Sorbitol is in turn converted into fructose with accompanied reduction of NAD+ by sorbitol dehydrogenase. Under normal circumstances, glucose is predominantly converted to glucose-6-phosphate by hexokinase and then enters the glycolytic pathway, whereas only a small amount of glucose is metabolized through the polyol pathway due to a relatively low affinity of ALR2 for this substrate. During hyperglycemia, the polyol metabolic pathway is activated and the increased flux of glucose through the polyol pathway triggers the accumulation of sorbitol, which mainly happens in tissues demonstrating insulin-independent uptake of glucose, such as lens, kidney, retina, and peripheral nerves |
-, 738838 |
| 1.1.1.2 | more |
structure homology model of AdhD and its mutants generated using the model of prostaglandin F synthase from Trypanosoma brucei (PDB ID 1VBJ, 40.26% identity). The homology models are aligned with the structure of 2,5-DKGR from Corynebacterium (PDB ID 1A80 with bound NADPH, and PDB ID 1M9H with bound NADH), overview |
746361 |
| 1.1.1.2 | physiological function |
ALR1 is present in all tissues and plays an important role in detoxification |
-, 738161 |
| 1.1.1.2 | physiological function |
bacterium Mycobacterium sp. B-009, is able to grow on racemic 1,2-propanediol. The strain oxidizes 3-methyl-1,5-pentanediol to 5-hydroxy-3-methyl-pentanoic acid via the S-form of 5-hydroxy-3-methyl-pentanoic acid. The enzyme is an enantioselective 3-methyl-1,5-pentanediol dehydrogenase |
737874 |
| 1.1.1.2 | physiological function |
enzyme is involved in swainsonine degradation, an indolizidine alkaloid |
-, 739731 |
| 1.1.1.2 | physiological function |
the physiological roles of the enzyme are proposed to be in the formation of alcohols such as ethanol or acetoin concomitant to the NADPH oxidation |
738511 |
| 1.1.1.2 | physiological function |
the proposed physiological role of NADP-dependent alcohol dehydrogenase in Pyrococcus furiosus is to both dispose of excess reducing equivalents and to detoxify the aldehydes produced by the fermentative pathways |
722498 |
| 1.1.1.2 | physiological function |
the specific activities of ADH, formate benzyl viologen oxidoreductase, and hydrogenase dramatically increase in cells grown under sulfur limitation. This is accompanied by increased amounts of H2 and alcohol (ethanol and butanol). Under S0 limitation, ADH may reduce to alcohols the aldehydes that are generated by fermentation, thereby serving to dispose of excess reductant |
-, 736339 |
