All-trans-retinol 13,14-reductase

RETSAT
Identifiers
Aliases	RETSAT, retinol saturase
External IDs	OMIM: 617597; MGI: 1914692; HomoloGene: 41195; GeneCards: RETSAT; OMA:RETSAT - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	85,354,531 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	72,585,408 bp
RNA expression pattern
	Top expressed in
	mucosa of transverse colon; ; mucosa of ileum; ; jejunal mucosa; ; rectum; ; duodenum; ; subcutaneous adipose tissue; ; right adrenal cortex; ; left adrenal gland; ; left adrenal cortex; ; abdominal fat;
	Top expressed in
	left lobe of liver; ; right kidney; ; duodenum; ; brown adipose tissue; ; human kidney; ; proximal tubule; ; epithelium of stomach; ; yolk sac; ; pyloric antrum; ; digastric muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	oxidoreductase activity; all-trans-retinol 13,14-reductase activity;
Cellular component	nuclear membrane; nuclear outer membrane; membrane; endoplasmic reticulum; endoplasmic reticulum membrane;
Biological process	retinol metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	54884
	67442
	ENSG00000042445
	ENSMUSG00000056666
	Q6NUM9
	Q64FW2
	NM_017750
	NM_026159
	NP_060220
	NP_080435
	Wikidata
View/Edit Human	View/Edit Mouse

Search
PMC	articles
PubMed	articles
NCBI	proteins

all-trans-retinol 13,14-reductase
all-trans-retinol 13,14-reductase
Identifiers
EC no.	1.3.99.23
CAS no.	418767-56-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

In enzymology, an all-trans-retinol 13,14-reductase (EC 1.3.99.23) is an enzyme, encoded by the RETSAT gene,^[5]^[6]^[7] that catalyzes the chemical reaction

all-trans-13,14-dihydroretinol + acceptor

\rightleftharpoons

all-trans-retinol + reduced acceptor

Thus, the two substrates of this enzyme are all-trans-13,14-dihydroretinol and acceptor, whereas its two products are all-trans-retinol and reduced acceptor. Under physiological conditions the reaction proceeds in the opposite direction catalyzing the saturation of the 13-14 double bond of all-trans-retinol.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase. Other names in common use include retinol saturase, RetSat, (13,14)-all-trans-retinol saturase, and all-trans-retinol:all-trans-13,14-dihydroretinol saturase.

The gene has also been called PPAR-alpha-regulated and starvation-induced gene protein.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000042445 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000056666 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A (Oct 2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
^ Moise AR, Kuksa V, Imanishi Y, Palczewski K (Nov 2004). "Identification of All-trans-Retinol:All-trans-13,14-dihydroretinol Saturase*". J Biol Chem. 279 (48): 50230–42. doi:10.1074/jbc.M409130200. PMC 2665716. PMID 15358783.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ "Entrez Gene: RETSAT retinol saturase (all-trans-retinol 13,14-reductase)".
^ "RETSAT - All-trans-retinol 13,14-reductase precursor - Homo sapiens (Human) - RETSAT gene & protein". www.uniprot.org. Retrieved 2017-11-05.

Moise AR, Kuksa V, Imanishi Y, Palczewski K (2004). "Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase". J. Biol. Chem. 279 (48): 50230–42. doi:10.1074/jbc.M409130200. PMC 2665716. PMID 15358783.{{cite journal}}: CS1 maint: unflagged free DOI (link)

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.

This EC 1.3 enzyme-related article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000042445 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000056666 – 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.

[pmid12975309-5] Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A (Oct 2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.

[pmid15358783-6] Moise AR, Kuksa V, Imanishi Y, Palczewski K (Nov 2004). "Identification of All-trans-Retinol:All-trans-13,14-dihydroretinol Saturase*". J Biol Chem. 279 (48): 50230–42. doi:10.1074/jbc.M409130200. PMC 2665716. PMID 15358783.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[entrez-7] "Entrez Gene: RETSAT retinol saturase (all-trans-retinol 13,14-reductase)".

[8] "RETSAT - All-trans-retinol 13,14-reductase precursor - Homo sapiens (Human) - RETSAT gene & protein". www.uniprot.org. Retrieved 2017-11-05.

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v t e Oxidoreductases: CH–CH oxidoreductases (EC 1.3)
1.3.1: NAD/NADP acceptor	Enoyl-acyl carrier protein reductase/Enoyl ACP reductase 7-Dehydrocholesterol reductase Biliverdin reductase 2,4 Dienoyl-CoA reductase Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase
1.3.3: Oxygen acceptor	Dihydroorotate dehydrogenase Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Bilirubin oxidase Acyl-CoA oxidase Dihydrouracil oxidase Tetrahydroberberine oxidase Secologanin synthase Tryptophan alpha,beta-oxidase Pyrroloquinoline-quinone synthase L-galactonolactone oxidase
1.3.5: Quinone	Succinate dehydrogenase SDHA SDHB SDHC SDHD
1.3.99: Other acceptors	Fumarate reductase Butyryl-CoA dehydrogenase Acyl CoA dehydrogenase ACADSB ACADS 5α-reductase SRD5A1 SRD5A2 SRD5A3 Glutaryl-CoA dehydrogenase Isovaleryl coenzyme A dehydrogenase 3-oxo-5beta-steroid 4-dehydrogenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

References

Further reading