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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: retinol dehydrogenase 3

Gene: DHRS3 Accession Number: HS08684 (MetaCyc)

Synonyms: UNQ2424/PRO4983, DD83.1, retinal short-chain dehydrogenase/reductase 1, retSDR1, short-chain dehydrogenase/reductase 3

Species: Homo sapiens

Summary:
General Background

The key enzymes involved in retinoid metabolisms are alcohol and aldehyde dehydrogenases that convert retinols to aldehydes and aldehydes to carboxylic acids, respectively. The first oxidation reaction is catalyzed by a large number of enzymes from the small-chain dehydrogenase/reductase (SDR) superfamily and by classic medium chain alcohol dehydrogenases. SDRs are weakly conserved in their primary sequences, with the exception of key residues involved in catalysis, nucleotide recognition, and members of closely related subfamilies. SDRs also display NADP or NAD cofactor preference and, if they are retinol dehydrogenases (RDHs), favor all-trans- or cis-retinol substrates. Some RDH enzymes also catalyze the oxidation of steroids in addition to retinols [Haeseleer02].

About This Enzyme

DHRS3 encodes a member of the SDR family that has been implicated as a retinol dehydrogenase.

Expression of the gene is broad, with highest levels found in heart, placenta, lung, liver, kidney, pancreas, thyroid, testis, stomach, trachea and spinal cord, and lower levels found in skeletal muscle, intestine and lymph node [Haeseleer98].

A cDNA encoding the enzyme has been cloned from a human retinal library and expressed in Escherichia coli and insect cells. The recombinant enzyme reduced all-trans-retinal but not 11-cis-retinal in the presence of NADPH. NADH could not substitute for NADPH [Haeseleer98].

Locations: membrane

Map Position: [12,444,308 <- 12,493,843]

Molecular Weight of Polypeptide: 33.548 kD (from nucleotide sequence)

Unification Links: ArrayExpress:O75911 , Entrez-gene:9249 , PhosphoSite:O75911 , PhylomeDB:O75911 , Pride:O75911 , Protein Model Portal:O75911 , SMR:O75911 , String:9606.ENSP00000365397 , UniProt:O75911

Relationship Links: InterPro:IN-FAMILY:IPR002198 , InterPro:IN-FAMILY:IPR002347 , InterPro:IN-FAMILY:IPR016040 , Pfam:IN-FAMILY:PF00106 , Prints:IN-FAMILY:PR00080 , Prints:IN-FAMILY:PR00081 , Prosite:IN-FAMILY:PS00061

Gene-Reaction Schematic: ?

Instance reactions of [allopregnanolone + NAD(P)+ ↔ 5-α-pregnane-3,20-dione + NAD(P)H + H+] (1.1.1.213):
i1: allopregnanolone + NAD+ → 5-α-pregnane-3,20-dione + NADH + H+ (1.1.-.-)

i2: allopregnanolone + NADP+ ← 5-α-pregnane-3,20-dione + NADPH + H+ (1.1.1.278)

GO Terms:

Biological Process: GO:0006631 - fatty acid metabolic process
GO:0007601 - visual perception
GO:0008152 - metabolic process
Molecular Function: GO:0000166 - nucleotide binding
GO:0016491 - oxidoreductase activity
Cellular Component: GO:0016021 - integral component of membrane

Credits:
Created 10-Aug-2011 by Caspi R , SRI International


Enzymatic reaction of: NADP-retinol dehydrogenase (retinol dehydrogenase 3)

EC Number: 1.1.1.300

all-trans-retinol + NADP+ <=> all-trans-retinal + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

In Pathways: the visual cycle I (vertebrates) , retinol biosynthesis

Exons/Introns:


References

Haeseleer02: Haeseleer F, Jang GF, Imanishi Y, Driessen CA, Matsumura M, Nelson PS, Palczewski K (2002). "Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina." J Biol Chem 277(47);45537-46. PMID: 12226107

Haeseleer98: Haeseleer F, Huang J, Lebioda L, Saari JC, Palczewski K (1998). "Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal." J Biol Chem 273(34);21790-9. PMID: 9705317


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, BIOCYC14A.