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Literature summary for 1.1.1.315 extracted from
- Structures important in NAD(P)(H) specificity for mammalian retinol and 11-cis-retinol dehydrogenases (1996), Biochem. Biophys. Res. Commun., 226, 118-127.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| alignment of Streptomyces hydrogenans 20beta-hydroxysteroid dehydrogenase with rat retinol dehydrogenase and cow 11-cis retinol dehydrogenase. Lysine64 of the rat enzyme is important in stabilizing binding of 2'-phosphate on NADP+ in two ways: lysine's positively charged side chain has a coulombic attraction to the 2'-phosphate and partially compensates for the negative charge of aspartic acid-38. Cow 11-cis retinol dehydrogenase has threonine61 at the position homologous to lysine64. Threonine61 does not have a stabilizing coulombic interaction with NADP+, nor can threonine61 counteract the repulsive interaction between NADP+ and aspartic acid37 in 11-cis retinol dehydrogenase | Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | aspartic acid37 and threonine61 are important in the specificity of 11-cis retinol dehydrogenase for NAD+ | Bos taurus |  |
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