EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.3.1.3 | enzyme in binary complex with product NADP+, containing two monomers of AKR1D1, each of which consists of a 325-residue polypeptide chain that adopts an (alpha/beta)8-barrel fold, the AKR1D1-NADP+ complex adopts an extended anti-conformation, X-ray diffraction structure determination and analysis at 1.79 A resolution, comparison with other enzyme binary and tertiary ligand complex structures, overview | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.1.3 | additional information | determination of AKR1D1 reaction mechanism by mutational analysis revealing that the 4-pro-R hydride is transferred from the re-face of the nicotinamide ring to C5 of the steroid substrate. E120, a unique substitution in the AKR catalytic tetrad, permits a deeper penetration of the steroid substrate into the active site to promote optimal reactant positioning. It participates with Y58 to create a superacidic oxyanion hole for polarization of the C3 ketone, no role for K87 in the proton relay, overview | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.1.3 | cholest-4-en-3-one + NADPH + H+ | Homo sapiens | - |
5beta-cholestan-3-one + NADP+ | - |
? | |
1.3.1.3 | cortisone + NADPH + H+ | Homo sapiens | - |
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ | - |
? | |
1.3.1.3 | progesterone + NADPH + H+ | Homo sapiens | - |
? | - |
? | |
1.3.1.3 | testosterone + NADPH + H+ | Homo sapiens | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.1.3 | Homo sapiens | P51857 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.3.1.3 | 17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH + H+ | reaction mechanism, overview | Homo sapiens | |
1.3.1.3 | 5beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+ | reaction mechanism, overview | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.1.3 | cholest-4-en-3-one + NADPH + H+ | - |
Homo sapiens | 5beta-cholestan-3-one + NADP+ | - |
? | |
1.3.1.3 | cortisone + NADPH + H+ | - |
Homo sapiens | 17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ | - |
? | |
1.3.1.3 | additional information | AKR1D1 catalyzes reduction of DELTA4-ene double bonds in steroid hormones and bile acid precursors. Determination of reaction mechanism by mutational analysis revealing that the 4-pro-R hydride is transferred from the re-face of the nicotinamide ring to C5 of the steroid substrate. E120, a unique substitution in the AKR catalytic tetrad, permits a deeper penetration of the steroid substrate into the active site to promote optimal reactant positioning. It participates with Y58 to create a superacidic oxyanion hole for polarization of the C3 ketone, no role for K87 in the proton relay, overview | Homo sapiens | ? | - |
? | |
1.3.1.3 | progesterone + NADPH + H+ | - |
Homo sapiens | ? | - |
? | |
1.3.1.3 | testosterone + NADPH + H+ | - |
Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.1.3 | AKR1D1 | - |
Homo sapiens |
1.3.1.3 | aldoketo reductase 1D1 | - |
Homo sapiens |
1.3.1.3 | steroid 5beta-reductase | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.1.3 | NADPH | - |
Homo sapiens |