Biology:Medium-chain acyl-CoA dehydrogenase
From HandWiki
| Medium-chain acyl-CoA dehydrogenase | |||||||||
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 Medium-chain acyl-CoA dehydrogenase tetramer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 1.3.8.7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Medium-chain acyl-CoA dehydrogenase (EC 1.3.8.7, fatty acyl coenzyme A dehydrogenase (ambiguous), acyl coenzyme A dehydrogenase (ambiguous), acyl dehydrogenase (ambiguous), fatty-acyl-CoA dehydrogenase (ambiguous), acyl CoA dehydrogenase (ambiguous), general acyl CoA dehydrogenase (ambiguous), medium-chain acyl-coenzyme A dehydrogenase, acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous), ACADM (gene name).) is an enzyme with systematic name medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction
- a medium-chain acyl-CoA + electron-transfer flavoprotein [math]\displaystyle{ \rightleftharpoons }[/math] a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
This enzyme contains FAD as prosthetic group and participates in fatty acid metabolism and PPAR signaling pathway.[9]
References
- ↑ "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochimica et Biophysica Acta 17 (2): 292–4. June 1955. doi:10.1016/0006-3002(55)90374-7. PMID 13239683.
- ↑ "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase". The Journal of Biological Chemistry 218 (2): 701–6. February 1956. doi:10.1016/S0021-9258(18)65836-3. PMID 13295224.
- ↑ Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
- ↑ "Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme". The Journal of Biological Chemistry 260 (2): 1311–25. January 1985. doi:10.1016/S0021-9258(20)71245-7. PMID 3968063.
- ↑ "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal 9 (9): 718–25. June 1995. doi:10.1096/fasebj.9.9.7601336. PMID 7601336.
- ↑ "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate". Proceedings of the National Academy of Sciences of the United States of America 90 (16): 7523–7. August 1993. doi:10.1073/pnas.90.16.7523. PMID 8356049. Bibcode: 1993PNAS...90.7523K.
- ↑ "Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules". Biochemistry 34 (45): 14942–53. November 1995. doi:10.1021/bi00045a039. PMID 7578106.
- ↑ "Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex". The Journal of Biological Chemistry 279 (31): 32904–12. July 2004. doi:10.1074/jbc.M404884200. PMID 15159392.
- ↑ "Downregulation of fatty acid oxidation by involvement of HIF-1α and PPARγ in human gastric adenocarcinoma and its related clinical significance". Journal of Physiology and Biochemistry 77 (2): 249–260. May 2021. doi:10.1007/s13105-021-00791-3. PMID 33730333. https://pubmed.ncbi.nlm.nih.gov/33730333/.
External links
- Medium-chain+acyl-CoA+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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