All-trans-retinol 13,14-reductase

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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
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IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
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PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
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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
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Last updated January 25, 2024

In enzymology, an all-trans-retinol 13,14-reductase (EC 1.3.99.23) is an enzyme, encoded by the RETSAT gene,^[1]^[2]^[3] 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.^[4]

Related Research Articles

QDPR is a human gene that produces the enzyme quinoid dihydropteridine reductase. This enzyme is part of the pathway that recycles a substance called tetrahydrobiopterin, also known as BH4. Tetrahydrobiopterin works with an enzyme called phenylalanine hydroxylase to process a substance called phenylalanine. Phenylalanine is an amino acid that is obtained through the diet; it is found in all proteins and in some artificial sweeteners. When tetrahydrobiopterin interacts with phenylalanine hydroxylase, tetrahydrobiopterin is altered and must be recycled to a usable form. The regeneration of this substance is critical for the proper processing of several other amino acids in the body. Tetrahydrobiopterin also helps produce certain chemicals in the brain called neurotransmitters, which transmit signals between nerve cells.

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

Retinal pigment epithelium-specific 65 kDa protein, also known as retinoid isomerohydrolase, is an enzyme of the vertebrate visual cycle that is encoded in humans by the RPE65 gene. RPE65 is expressed in the retinal pigment epithelium and is responsible for the conversion of all-trans-retinyl esters to 11-cis-retinol during phototransduction. 11-cis-retinol is then used in visual pigment regeneration in photoreceptor cells. RPE65 belongs to the carotenoid oxygenase family of enzymes.

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

GPI transamidase component PIG-T is an enzyme that in humans is encoded by the PIGT gene.

Scavenger mRNA-decapping enzyme DcpS is a protein that in humans is encoded by the DCPS gene.

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

DNA primase large subunit is an enzyme that in humans is encoded by the PRIM2 gene.

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

Dehydrogenase/reductase SDR family member 1, also known as Short chain dehydrogenase/reductase family 19C member 1 is an enzyme that in humans is encoded by the DHRS1 gene located on chromosome 14.

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

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

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

Retinol dehydrogenase 8 is an enzyme that in humans is encoded by the RDH8 gene.

Dehydrogenase/reductase SDR family member 4 is an enzyme that in humans is encoded by the DHRS4 gene.

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.

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

Ribonucleoside-diphosphate reductase subunit M2, also known as ribonucleotide reductase small subunit, is an enzyme that in humans is encoded by the RRM2 gene.

NADP-retinol dehydrogenase (EC 1.1.1.300, all-trans retinal reductase, all-trans-retinol dehydrogenase, NADP(H)-dependent retinol dehydrogenase/reductase, RDH11, RDH12, RDH13, RDH14, retinol dehydrogenase 12, retinol dehydrogenase 14, retinol dehydrogenase (NADP⁺), RalR1, PSDR1) is an enzyme with systematic name retinol:NADP⁺ oxidoreductase. This enzyme catalyses the following chemical reaction

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.

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.
↑ "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.

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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.434..724H. 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.

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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.

[entrez-3] "Entrez Gene: RETSAT retinol saturase (all-trans-retinol 13,14-reductase)".

[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)

All-trans-retinol 13,14-reductase

Related Research Articles

References

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