From Wikipedia, the free encyclopedia
Medium-chain acyl-CoA dehydrogenase
Medium-chain acyl-CoA dehydrogenase tetramer, Human
Identifiers
EC no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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 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

  1. ^ Crane FL, Hauge JG, Beinert H (June 1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochimica et Biophysica Acta. 17 (2): 292–4. doi: 10.1016/0006-3002(55)90374-7. PMID  13239683.
  2. ^ Crane FL, Mii S, Hauge JG, Green DE, Beinert H (February 1956). "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. doi: 10.1016/S0021-9258(18)65836-3. PMID  13295224.
  3. ^ Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. (eds.). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
  4. ^ Ikeda Y, Okamura-Ikeda K, Tanaka K (January 1985). "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. doi: 10.1016/S0021-9258(20)71245-7. PMID  3968063.
  5. ^ Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718–25. doi: 10.1096/fasebj.9.9.7601336. PMID  7601336. S2CID  42549744.
  6. ^ Kim JJ, Wang M, Paschke R (August 1993). "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. Bibcode: 1993PNAS...90.7523K. doi: 10.1073/pnas.90.16.7523. PMC  47174. PMID  8356049.
  7. ^ Peterson KL, Sergienko EE, Wu Y, Kumar NR, Strauss AW, Oleson AE, Muhonen WW, Shabb JB, Srivastava DK (November 1995). "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. doi: 10.1021/bi00045a039. PMID  7578106.
  8. ^ Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D (July 2004). "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. doi: 10.1074/jbc.M404884200. PMID  15159392.
  9. ^ Ezzeddini R, Taghikhani M, Salek Farrokhi A, Somi MH, Samadi N, Esfahani A, Rasaee, MJ (May 2021). "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. doi: 10.1007/s13105-021-00791-3. PMID  33730333. S2CID  232300877.

External links

From Wikipedia, the free encyclopedia
Medium-chain acyl-CoA dehydrogenase
Medium-chain acyl-CoA dehydrogenase tetramer, Human
Identifiers
EC no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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 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

  1. ^ Crane FL, Hauge JG, Beinert H (June 1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochimica et Biophysica Acta. 17 (2): 292–4. doi: 10.1016/0006-3002(55)90374-7. PMID  13239683.
  2. ^ Crane FL, Mii S, Hauge JG, Green DE, Beinert H (February 1956). "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. doi: 10.1016/S0021-9258(18)65836-3. PMID  13295224.
  3. ^ Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. (eds.). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
  4. ^ Ikeda Y, Okamura-Ikeda K, Tanaka K (January 1985). "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. doi: 10.1016/S0021-9258(20)71245-7. PMID  3968063.
  5. ^ Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718–25. doi: 10.1096/fasebj.9.9.7601336. PMID  7601336. S2CID  42549744.
  6. ^ Kim JJ, Wang M, Paschke R (August 1993). "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. Bibcode: 1993PNAS...90.7523K. doi: 10.1073/pnas.90.16.7523. PMC  47174. PMID  8356049.
  7. ^ Peterson KL, Sergienko EE, Wu Y, Kumar NR, Strauss AW, Oleson AE, Muhonen WW, Shabb JB, Srivastava DK (November 1995). "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. doi: 10.1021/bi00045a039. PMID  7578106.
  8. ^ Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D (July 2004). "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. doi: 10.1074/jbc.M404884200. PMID  15159392.
  9. ^ Ezzeddini R, Taghikhani M, Salek Farrokhi A, Somi MH, Samadi N, Esfahani A, Rasaee, MJ (May 2021). "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. doi: 10.1007/s13105-021-00791-3. PMID  33730333. S2CID  232300877.

External links


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