EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.3.1.3 | the crystal structure of the 5beta-POR-NADP+ binary complex reveals that 5beta-POR exhibits a characteristic short-chain dehydrogenase fold with an N-terminal domain consisting of a double Rossmann fold for cofactor binding and an insertional domain between strands betaF and betaG of about 100 residues for substrate binding, crystal structure of the 5beta-POR-NADP+ binary complex reveals that the side chain of K147 is found in a similar position to the lysine residue of the YXX(S)K motif in standard short-chain dehydrogenases | Digitalis lanata |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.1.3 | additional information | Digitalis lanata | AKR1D1 catalyzes the stereospecific reduction of the delta4-double-bond of circulating steroid hormones that contain the delta4-3-ketosteroid functionality, e.g. the reduction of testosteron, progesterone and cortisol to yield the corresponding 5-dihydrosteroid | ? | - |
? | |
1.3.1.3 | additional information | Digitalis lanata | aldo-keto reductases are a major superfamily of monomeric NADPH-dependent carbonyl oxidoreductases, active site contains conserved residues D50, Y55, K84, and H117 | ? | - |
? | |
1.3.1.3 | additional information | Digitalis lanata | the steroid 5beta-reductases catalyze a reaction that is unique in steroid enzymology since the resultant product contains a cis-A/B ring configuration and accordingly contains a 90° bend, the cis-A/B ring configuration is an essential characteristic of cardiac glycosides, e.g. digioxin and bile acids and their precursors | ? | - |
? | |
1.3.1.3 | progesterone + NADPH + H+ | Digitalis lanata | stereospecific reduction of the 4-double-bond in cardenolide biosynthesis | 5beta-pregnane-3,20-dione + NADP+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.1.3 | Digitalis lanata | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.1.3 | additional information | AKR1D1 catalyzes the stereospecific reduction of the delta4-double-bond of circulating steroid hormones that contain the delta4-3-ketosteroid functionality, e.g. the reduction of testosteron, progesterone and cortisol to yield the corresponding 5-dihydrosteroid | Digitalis lanata | ? | - |
? | |
1.3.1.3 | additional information | aldo-keto reductases are a major superfamily of monomeric NADPH-dependent carbonyl oxidoreductases, active site contains conserved residues D50, Y55, K84, and H117 | Digitalis lanata | ? | - |
? | |
1.3.1.3 | additional information | the steroid 5beta-reductases catalyze a reaction that is unique in steroid enzymology since the resultant product contains a cis-A/B ring configuration and accordingly contains a 90° bend, the cis-A/B ring configuration is an essential characteristic of cardiac glycosides, e.g. digioxin and bile acids and their precursors | Digitalis lanata | ? | - |
? | |
1.3.1.3 | progesterone + NADPH + H+ | stereospecific reduction of the 4-double-bond in cardenolide biosynthesis | Digitalis lanata | 5beta-pregnane-3,20-dione + NADP+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.1.3 | 5beta-POR | - |
Digitalis lanata |
1.3.1.3 | AKR1D1 | - |
Digitalis lanata |
1.3.1.3 | aldo-keto reductase | - |
Digitalis lanata |
1.3.1.3 | steroid 5beta-reductase | - |
Digitalis lanata |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.1.3 | NAD(P)H | - |
Digitalis lanata |