Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.300 extracted from

  • Belyaeva, O.V.; Adams, M.K.; Popov, K.M.; Kedishvili, N.Y.
    Generation of retinaldehyde for retinoic acid biosynthesis (2019), Biomolecules, 10, 5 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8IZV5
-
-
Mus musculus Q8VCH7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
retinal + NADPH + H+ reaction of the retinoid oxidoreductive complex (ROC) composed of RDH10 (SDR16C4)and DHRS3 (EC 1.2.1.36) Homo sapiens retinol + NADP+
-
ir
retinal + NADPH + H+ reaction of the retinoid oxidoreductive complex (ROC) composed of RDH10 (SDR16C4)and DHRS3 (EC 1.2.1.36) Mus musculus retinol + NADP+
-
ir
retinol + NAD+ reaction of RDH10 (SDR16C4) Homo sapiens retinal + NADH + H+
-
ir
retinol + NAD+ reaction of RDH10 (SDR16C4) Mus musculus retinal + NADH + H+
-
ir

Synonyms

Synonyms Comment Organism
RDH10
-
Homo sapiens
RDH10
-
Mus musculus
retinol dehydrogenase 10
-
Homo sapiens
retinol dehydrogenase 10
-
Mus musculus
SDR16C4
-
Homo sapiens
SDR16C4
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
NAD+
-
Mus musculus
NADH
-
Homo sapiens
NADH
-
Mus musculus
NADP+
-
Homo sapiens
NADP+
-
Mus musculus
NADPH
-
Homo sapiens
NADPH
-
Mus musculus

General Information

General Information Comment Organism
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 Homo sapiens
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 Mus musculus
malfunction mutagenesis and targeted gene knockout studies in mice confirm that a functional RDH10 is critical for survival until embryonic day 11.5 (E11.5), as Rdh10-/- embryos can be rescued by maternal supplementation of retinaldehyde from E7.5 to E11.5. Genetic disruption of murine Rdh10 gene results in a marked reduction in retinoic acid (RA) synthesis that leads to numerous developmental abnormalities. RDH10-deficient embryos display defects in axial extension and embryonic turning, abnormal hindbrain and craniofacial patterning, agenesis of posterior pharyngeal arches, perturbed somitogenesis, hypoplastic forelimb buds, and abnormal organogenesis of multiple systems, including heart and vasculature, lungs, and gastrointestinal tract. Embryos carrying a targeted knockout of Rdh10 died by E12.5, while embryos carrying various mutant alleles survived until E13.5-E15.5, or until late gestation. Testicular cell-specific conditional knockout of Rdh10 shows that deficiency of RDH10 in both Sertoli and germ cells completely impairs testicular RA signaling in juvenile animals. Spermatogenesis progressively recovers in adult Rdh10 conditional knockout mice, suggesting that RDH10 is not essential for adult spermatogenesis. In mice, targeted knockout of Dhrs3 results in an about 30% increase in RA levels, reduction in the levels of retinol and retinyl esters, and embryonic lethality late in gestation Mus musculus
malfunction mutations in the gene encoding retinol dehydrogenase 10 (Rdh10) lead to craniofacial, limb, and organ abnormalities. This phenotype, called RDH10trex, is caused by the severely reduced ability of mutant RDH10 to oxidize retinol to retinaldehyde, resulting in insufficient RA signaling Homo sapiens
metabolism the enzyme is involved in retinoic acid biosynthesis, overview. Retinoic acid (RA)-mediated transcriptional feedback loops upregulate the expression of the reductive enzyme DHRS3 and downregulate the expression of the oxidative enzyme RDHE2 in response to an increase in retinoic acid levels. Members of two families of SDRs are involved in the regulation of RA homeostasis, SDR16C and SDR7C. Regulation of the flux from retinol to retinaldehyde Homo sapiens
metabolism the enzyme is involved in retinoic acid biosynthesis, overview. Retinoic acid (RA)-mediated transcriptional feedback loops upregulate the expression of the reductive enzyme DHRS3 and downregulate the expression of the oxidative enzyme RDHE2 in response to an increase in retinoic acid levels. Members of two families of SDRs are involved in the regulation of RA homeostasis, SDR16C and SDR7C. Regulation of the flux from retinol to retinaldehyde Mus musculus
physiological function the enzyme is involved in retinoic acid biosynthesis, overview. The NAD(H)-dependent oxidoreductases usually function in the oxidative direction in intact cells, whereas the NADP(H)-dependent enzyme function in the reductive direction. RDH10 acts as a high-affinity retinol dehydrogenase with a preference for NAD+ as cofactor. DHRS3 acts as an NADP(H)-dependent retinaldehyde reductase Mus musculus
physiological function the enzyme is involved in retinoic acid biosynthesis, overview. 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. RDH10 acts as a high-affinity retinol dehydrogenase with a preference for NAD+ as cofactor Homo sapiens