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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
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PubMed	articles
NCBI	proteins

All-trans-retinol 13,14-reductase
Identifiers
Aliases	(13,14)-all-trans-retinol saturaseRetSatall-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductaseall-trans-retinol:all-trans-13,14-dihydroretinol saturaseretinol saturase
External IDs	GeneCards: ; OMA:- orthologs
Orthologs
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	n ; a
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	Wikidata
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All-trans-retinol 13,14-reductase

Last updated January 31, 2026

In enzymology, all-trans-retinol 13,14-reductase (EC 1.3.99.23) is an enzyme, encoded by the RETSAT gene,^[1]^[2] that catalyzes the chemical reaction

retinol

+ reduced acceptor

13,14-dihydroretinol

+ electron acceptor

The enzyme acts on retinol (vitamin A) to reduce it to 13,14-dihydroretinol. Its is not known to be able to catalyze reaction in the opposite direction.^[3]

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.^[4]

References

↑ 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.
↑ Enzyme 1.3.99.23 at KEGG Pathway Database.
↑ "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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[pmid12975309-1] 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.

[pmid15358783-2] 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.

[3] Enzyme 1.3.99.23 at KEGG Pathway Database.

[4] "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)