EC Number   |
General Information |
Reference  |
|---|
   1.1.1.300 | physiological function |
Rdh11 is able to efficiently detoxify 4-hydroxynonenal in cells. Rdh11 protects against 4-hydroxynonenal modification of proteins and 4-hydroxynonenal-induced apoptosis in HEK-293 cells |
712068 |
| 1.1.1.300 | physiological function |
Rdh12 is able to efficiently detoxify 4-hydroxynonenal in cells, most probably through its ability to reduce it to a nontoxic alcohol. Cells expressing Rdh12 show significantly less formation of Michael adducts with lysine, histidine, or cysteine residues of proteins thereby inhibiting their physiological functions. Microsomes from retinas of Rdh12 knockout mice form significantly more Michael adducts with microsomal proteins in the presence of 4-hydroxynonenal than wild-type. RDH12 also protects against light-induced apoptosis of photoreceptors |
712068 |
| 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 | malfunction |
loss-of-function mutations of RDH12 cause retinal degeneration in some forms of Leber congenital amaurosis. Outer segments of rods deficient in Rdh12 show no altered phenotype. Following exposure to light, a leak of retinoids from outer to inner segments is detected in rods from both wild-type and knock-out mice. In cells lacking Rdh8, EC 1.1.1.105, or Rdh12, this leak is mainly all-trans-retinal, overview. Retinal reductase activity is lost in RDH8-deficient mutants |
-, 722769 |
| 1.1.1.300 | physiological function |
RDH12 activity in the photoreceptor inner segments is also key enzyme function. RDH12 in inner segments can protect vital cell organelles against aldehyde toxicity caused by an intracellular leak of all-trans-retinal, as well as other aldehydes originating both inside and outside the cell |
-, 722769 |
| 1.1.1.300 | malfunction |
generation of Rdh13 knockout mice. No obvious difference in phenotype or function between Rdh13 knockout and wild-type mice. But in Rdh13-/- mice subjected to intense light exposure, the photoreceptor outer-plus-inner-segment and outer nuclear layer are dramatically shorter, and the amplitudes of a- and b-waves under scotopic conditions are significantly attenuated. Increased expression levels of CytC, CytC-responsive apoptosis proteinase activating factor-1 and caspases 3, and other mitochondria apoptosis-related genes, e.g. nuclear factor-kappa B P65 and B-cell lymphoma 2-associated X protein, are observed in Rdh13-/- mice |
-, 723236 |
| 1.1.1.300 | physiological function |
DHRS3 activity requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. The retinol dehydrogenase activity of RDH10 is reciprocally activated by retinaldehyde reductase DHRS3. At E13.5, DHRS3-null embryos have 4fold lower levels of retinol and retinyl esters, but only slightly elevated levels of retinoic acid. The membrane-associated retinaldehyde reductase and retinol dehydrogenase activities are decreased by 4- and 2fold, respectively, in Dhrs3-/- embryos, and Dhrs3-/- mouse embryonic fibroblasts exhibit reduced metabolism of both retinaldehyde andretinol. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other |
738610 |
| 1.1.1.300 | physiological function |
the retinol dehydrogenase activity of RDH10 is activated by retinaldehyde reductase DHRS3. In turn, DHRS3 requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other |
738610 |
| 1.1.1.300 | physiological function |
the retinol dehydrogenase activity of RDH10 is reciprocally activated by retinaldehyde reductase DHRS3. At E13.5, DHRS3-null embryos have 4fold lower levels of retinol and retinyl esters, but only slightly elevated levels of retinoic acid. The membrane-associated retinaldehyde reductase and retinol dehydrogenase activities are decreased by 4- and 2fold, respectively, in Dhrs3-/- embryos, and Dhrs3-/- mouse embryonic fibroblasts exhibit reduced metabolism of both retinaldehyde andretinol. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other |
738610 |
| 1.1.1.300 | physiological function |
energy status regulates all-trans-retinoic acid biosynthesis at the rate-limiting step, catalyzed by retinol dehydrogenases. Six h after re-feeding, isoform Rdh10 expression is decreased 4563% in liver, pancreas, and kidney, relative to mice fasted 16 h. All-trans-retinoic acid in the liver is decreased 44% 3 h after reduced Rdh expression. Oral gavage with glucose or injection with insulin decreases Rdh10 mRNA 50% or greater in mouse liver |
738670 |
