Crystallization (Comment) | Organism |
---|---|
at 22°C by vapor-diffusion using the hanging drop method. ALR1 in ternary complex with the coenzyme NADPH and 3,5-dichlorosalicylic acid, at a resolution of 2.41 A | Sus scrofa |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
20alpha-hydroxysteroid dehydrogenase | competitive inhibition, the inhibitor forms a 10fold stronger binding interaction with the catalytic residue (Tyr55), non-conserved hydrogen bonding interaction with His222, and additional van der Waals contacts with the non-conserved C-terminal residues Leu306, Leu308 and Phe311 that contribute to the inhibitor's selectivity advantage for 20alpha-hydroxysteroid dehydrogenase over 3,5-dichlorosalicylic acid | Sus scrofa | |
3,5-dichlorosalicylic acid | mixed type of competitive and non-competitive patterns with respect to the substrate. The inhibitor forms a network of hydrogen bonds with the active site residues Trp22, Tyr50, His113, Trp114 and Arg312. Is a less potent inhibitor of ALR1 (256fold) when compared to 20alpha-hydroxysteroid dehydrogenase | Sus scrofa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | P50578 | - |
- |
Purification (Comment) | Organism |
---|---|
to homogeneity | Sus scrofa |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | - |
Sus scrofa | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DL-glyceraldehyde + NADPH + H+ | - |
Sus scrofa | glycerol + NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
aldehyde reductase | - |
Sus scrofa |
ALR1 | - |
Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Sus scrofa |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.000044 | - |
- |
Sus scrofa | 20alpha-hydroxysteroid dehydrogenase | |
0.011 | - |
- |
Sus scrofa | 3,5-dichlorosalicylic acid |