EC Number   |
General Information |
Reference |
|---|
   1.1.1.300 | evolution |
all three proteins (Rdh11/12-like 1-3) include conserved signatures of the SDR family, such as cofactor binding (TGXXXGXG), the catalytic mechanism (YXXXK), and the structural integrity (NVG or NAG) patterns. Japanese eel Rdh11/12-like 1 clusters with piscine Rdh11 and Rdh12, however the cluster is formed outside that of mammalian Rdh11 and Rdh12. In contrast, Rdh11/12-like 2 and Rdh11/12-like 3 form a clade with putative European eel Rdh11s and Rdh12s outside that of mammalian and piscine Rdh11/Rdh12 |
761195 |
| 1.1.1.300 | evolution |
enzyme RDH10 belongs to the 16C family of the short-chain dehydrogenase/reductase (SDR) superfamily. Most members of the SDR16C family (except for DHRS3) exhibit higher binding affinities for NAD(H) as cofactor, whereas members of the SDR7C family prefer NADP(H). The NAD(H)-dependent oxidoreductases usually function in the oxidative direction in intact cells, whereas the NADP(H)-dependent enzymes function in the reductive direction |
760674 |
| 1.1.1.300 | evolution |
human retinol dehydrogenase 11 RDH11 belongs to the short-chain dehydrogenases/ reductases (SDR) family |
762061 |
| 1.1.1.300 | evolution |
RDH11 is co-expressed with BCO1 in several mouse tissues, and the retinaldehyde reductase activity of RDH11 is conserved in the mouse enzyme |
761488 |
| 1.1.1.300 | evolution |
RDHs that catalyze the interconversion of retinal and retinol involved in rhodopsin turnover are members of the family of short chain dehydrogenase/reductases |
722769 |
| 1.1.1.300 | evolution |
retinol dehydrogenase 11 (RDH11) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. A mild reduction in retinoic acid signaling is observed in RDH11-null testis |
761488 |
| 1.1.1.300 | evolution |
retinol dehydrogenase-10 (RDH10) is a member of the short-chain dehydrogenase/reductase family |
762073 |
| 1.1.1.300 | evolution |
retinol dehydrogenases (RDHs) are members of the short chain dehydrogenases/reductases (SDR) family of enzymes. The SDRs are typically 250-350 amino acids in length and have a relatively low sequence similarity of about 15-30%. Common to all SDRs is the highly conserved Rossman fold, which is composed of a central beta-sheet flanked by 3-4 alpha-helices, forming the cofactor binding site. The SDRs have two conserved domains: the cofactor binding site (GXXXGXG) and the catalytic site (YXXXK) |
761045 |
| 1.1.1.300 | evolution |
the enzyme belongs to the the short-chain dehydrogenase/reductase (SDR) superfamily, NAD(P)-dependent enzymes, and short-chain dehydrogenase/reductase 16C family (SDR16C) |
761818 |
| 1.1.1.300 | malfunction |
cyclic-light-reared Rdh8-/- knockout mice show elevated levels of all-trans retinal, contributing to RPE lipofuscin formation and accumulation. Lipofuscin accumulates in the retinal pigment epithelium (RPE) of Rdh8-/- mice |
761323 |
