EC Number   |
General Information |
Reference |
|---|
    1.3.1.3 | evolution |
the enzyme belongs to the aldoketo reductase (AKR) family, sequence comparisons, overview |
726120 |
| 1.3.1.3 | evolution |
the enzyme is a member of the aldo-keto reductase (AKR) family |
724713 |
| 1.3.1.3 | malfunction |
deficient 5beta-reductase activity can lead to cholestasis and neo-natal liver failure and is often lethal if it remains untreated |
724713 |
| 1.3.1.3 | more |
existence of a small alternative substrate binding pocket, structure-activity relationship, overview |
726492 |
| 1.3.1.3 | more |
residues Tyr156, Asp205, and Ser248 are responsible for the low catalytic efficiency of the enzyme, substrate binding pocket structure, overview |
726120 |
| 1.3.1.3 | more |
structure-function relationship, overview |
725399 |
| 1.3.1.3 | more |
the enzyme shows high catalytic efficiency |
726120 |
| 1.3.1.3 | physiological function |
human steroid 5beta-reductase, i.e. aldo-keto reductase 1D1, catalyzes the stereospecific NADPH-dependent reduction of the C4-C5 double bond of DELTA4-ketosteroids to yield an A/B cis-ring junction. This cis configuration is crucial for bile acid biosynthesis and plays important roles in steroid metabolism. AKR1D1 is the only enzyme necessary for all the 5-steroid metabolites present in humans |
726492 |
| 1.3.1.3 | physiological function |
the enzyme is responsible for steroid hormone 5beta-reduction, as well as for cholic acid and chenodeoxycholic bile-acid synthesis |
706774 |
| 1.3.1.3 | physiological function |
the human enzyme, AKR1D1, plays an essential role in bile-acid biosynthesis since the 5beta-configuration is required for the emulsifying properties of bile |
724713 |
