RDH8

Last updated
RDH8
Identifiers
Aliases RDH8 , PRRDH, SDR28C2, retinol dehydrogenase 8 (all-trans), retinol dehydrogenase 8
External IDs OMIM: 608575 MGI: 2685028 HomoloGene: 41062 GeneCards: RDH8
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_015725

NM_001030290

RefSeq (protein)

NP_056540

NP_001025461

Location (UCSC) Chr 19: 10.01 – 10.02 Mb Chr 9: 20.73 – 20.74 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Retinol dehydrogenase 8 is an enzyme that in humans is encoded by the RDH8 gene. [5] [6] [7]

All-trans-retinol dehydrogenase (RDH8) is a visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol in the presence of NADPH. [5] It is a member of the short chain dehydrogenase/reductase family and is located in the outer segments of the photoreceptor cells; hence it is also known as photoreceptor retinol dehydrogenase. It is important in the visual cycle by beginning the rhodopsin regeneration pathway by reducing all-trans-retinal, the product of bleached and hydrolysed rhodopsin. [8] This is a rate-limiting step in the visual cycle. [9] [supplied by OMIM] [7]

Related Research Articles

<span class="mw-page-title-main">Retinal</span> Chemical compound

Retinal is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision).

The visual cycle is a process in the retina that replenishes the molecule retinal for its use in vision. Retinal is the chromophore of most visual opsins, meaning it captures the photons to begin the phototransduction cascade. When the photon is absorbed, the 11-cis retinal photoisomerizes into all-trans retinal as it is ejected from the opsin protein. Each molecule of retinal must travel from the photoreceptor cell to the RPE and back in order to be refreshed and combined with another opsin. This closed enzymatic pathway of 11-cis retinal is sometimes called Wald's visual cycle after George Wald (1906–1997), who received the Nobel Prize in 1967 for his work towards its discovery.

In enzymology, a retinol dehydrogenase (RDH) (EC 1.1.1.105) is an enzyme that catalyzes the chemical reaction

In enzymology, an all-trans-retinol 13,14-reductase is an enzyme, encoded by the RETSAT gene, that catalyzes the chemical reaction

<span class="mw-page-title-main">Retinal G protein coupled receptor</span> Protein-coding gene in the species Homo sapiens

RPE-retinal G protein-coupled receptor also known as RGR-opsin is a protein that in humans is encoded by the RGR gene. RGR-opsin is a member of the rhodopsin-like receptor subfamily of GPCR. Like other opsins which bind retinaldehyde, it contains a conserved lysine residue in the seventh transmembrane domain. RGR-opsin comes in different isoforms produced by alternative splicing.

<span class="mw-page-title-main">SAG (gene)</span>

S-arrestin is a protein that in humans is encoded by the SAG gene.

<span class="mw-page-title-main">RDH5</span> Protein-coding gene in the species Homo sapiens

11-cis retinol dehydrogenase is an enzyme that in humans is encoded by the RDH5 gene.

<span class="mw-page-title-main">ARR3</span> Protein-coding gene in humans

Arrestin-C, also known as retinal cone arrestin-3, is a protein that in humans is encoded by the ARR3 gene.

<span class="mw-page-title-main">ADH4</span> Protein-coding gene in the species Homo sapiens

Alcohol dehydrogenase 4 is an enzyme that in humans is encoded by the ADH4 gene.

<span class="mw-page-title-main">GNGT1</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(T) subunit gamma-T1 is a protein that in humans is encoded by the GNGT1 gene. Either GNGT1 or GNGT2 is the gamma subunit (Gγ) of the Gβγ part of transducin, a heterotrimeric G-protein naturally expressed in vertebrate retina rod and cone cells. GNGT1 only occurs in rod cells, and GNGT2 only occurs in cone cells, with a different alpha (Gα) subunit.

<span class="mw-page-title-main">RDH11</span> Protein-coding gene in the species Homo sapiens

Retinol dehydrogenase 11 is an enzyme that in humans is encoded by the RDH11 gene.

<span class="mw-page-title-main">RDH12</span> Protein-coding gene in the species Homo sapiens

Retinol dehydrogenase 12 is an enzyme that in humans is encoded by the RDH12 gene.

<span class="mw-page-title-main">RDH14</span> Protein-coding gene in the species Homo sapiens

Retinol dehydrogenase 14 is an enzyme that in humans is encoded by the RDH14 gene.

<span class="mw-page-title-main">DHRS3</span> Protein-coding gene in the species Homo sapiens

Short-chain dehydrogenase/reductase 3 is an enzyme that in humans is encoded by the DHRS3 gene.

<span class="mw-page-title-main">DHRS9</span> Protein-coding gene in the species Homo sapiens

Dehydrogenase/reductase SDR family member 9 is an enzyme that in humans is encoded by the DHRS9 gene.

<span class="mw-page-title-main">HSD17B6</span>

Hydroxysteroid 17-beta dehydrogenase 6 is an enzyme that in humans is encoded by the HSD17B6 gene.

<span class="mw-page-title-main">CYP27C1</span> Protein-coding gene in the species Homo sapiens

CYP27C1 is a protein that in humans is encoded by the CYP27C1 gene. The Enzyme Commission number (EC) for this protein is EC 1.14.19.53. The full accepted name is all-trans-retinol 3,4-desaturase and the EC number 1 classifies CYP27C1 as a oxidoreductase that acts on paired donor by reducing oxygen. It is also identifiable by the UniProt code Q4G0S4.

<span class="mw-page-title-main">Lecithin retinol acyltransferase</span> Mammalian protein found in Homo sapiens

Lecithin retinol acyltransferase is an enzyme that in humans is encoded by the LRAT gene.

<span class="mw-page-title-main">RDH13</span> Protein-coding gene in the species Homo sapiens

Retinol dehydrogenase 13 (all-trans/9-cis) is a protein that in humans is encoded by the RDH13 gene. This gene encodes a mitochondrial short-chain dehydrogenase/reductase, which catalyzes the reduction and oxidation of retinoids. The encoded enzyme may function in retinoic acid production and may also protect the mitochondria against oxidative stress. Alternatively spliced transcript variants have been described.

<span class="mw-page-title-main">Emixustat</span> Chemical compound

Emixustat is a small molecule notable for its establishment of a new class of compounds known as visual cycle modulators (VCMs). Formulated as the hydrochloride salt, emixustat hydrochloride, it is the first synthetic medicinal compound shown to affect retinal disease processes when taken by mouth. Emixustat was invented by the British-American chemist, Ian L. Scott, and is currently in Phase 3 trials for dry, age-related macular degeneration (AMD).

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000080511 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000053773 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Rattner A, Smallwood PM, Nathans J (May 2000). "Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol". J Biol Chem. 275 (15): 11034–11043. doi: 10.1074/jbc.275.15.11034 . PMID   10753906.
  6. Persson B, Kallberg Y, Bray JE, et al. (Feb 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1–3): 94–98. Bibcode:2009CBI...178...94P. doi:10.1016/j.cbi.2008.10.040. PMC   2896744 . PMID   19027726.
  7. 1 2 "Entrez Gene: RDH8 retinol dehydrogenase 8 (all-trans)".
  8. Rando RR (2001). "The biochemistry of the visual cycle". Chem. Rev. 101 (7): 1881–1896. doi:10.1021/cr960141c. PMID   11710234.
  9. Saari JC, Garwin GG, Van Hooser JP, et al. (1998). "Reduction of all-trans-retinal limits regeneration of visual pigment in mice". Vision Res. 38 (10): 1325–1333. doi:10.1016/S0042-6989(97)00198-3. PMID   9667000. S2CID   16267177.

Further reading