Biology:All-trans-retinol 13,14-reductase
 Generic protein structure example |
| all-trans-retinol 13,14-reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.3.99.23 | ||||||||
| CAS number | 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 | ||||||||
| |||||||||
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 [math]\displaystyle{ \rightleftharpoons }[/math] 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]
References
- ↑ "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. Oct 2003. doi:10.1101/gr.1293003. PMID 12975309.
- ↑ "Identification of All-trans-Retinol:All-trans-13,14-dihydroretinol Saturase*". J Biol Chem 279 (48): 50230–42. Nov 2004. doi:10.1074/jbc.M409130200. PMID 15358783.
- ↑ "Entrez Gene: RETSAT retinol saturase (all-trans-retinol 13,14-reductase)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54884.
- ↑ "RETSAT - All-trans-retinol 13,14-reductase precursor - Homo sapiens (Human) - RETSAT gene & protein" (in en). https://www.uniprot.org/uniprot/Q6NUM9.
- "Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase". J. Biol. Chem. 279 (48): 50230–42. 2004. doi:10.1074/jbc.M409130200. PMID 15358783.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature 434 (7034): 724–31. 2005. doi:10.1038/nature03466. PMID 15815621. Bibcode: 2005Natur.434..724H.
- "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. 2007. doi:10.1093/dnares/12.2.117. PMID 16303743.
 |  |
