Acyl-CoA dehydrogenase
Oxford Dictionary of Biochemistry:
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acyl-CoA dehydrogenase
the first enzyme of fatty acid oxidation, responsible for catalysing an FAD-dependent alpha-beta dehydrogenation of a fatty acyl-CoA substrate. Four enzymes are recognized in humans. Very-long-chain acyl-CoA dehydrogenase (EC 1.3.99, abbr.: VLCAD) is a homodimer attached to the inner mitochondrial membrane in liver, and acts on fatty acids of chain length 14 — 20 carbon atoms. Its gene locus at 17p13 encodes a sequence of 655 amino acids. Long-chain acyl-CoA dehydrogenase (EC 1.3.99.13, abbr.: LCAD) is a homotetramer bound to the inner mitochondrial membrane that acts on fatty acids 12 — 18 carbon atoms long; it also has 2-enoyl-CoA hydratase activity and constitutes the α subunits of mitochondrial trifunctional protein (an α4β4 octamer). The β subunits of the trifunctional protein have 3-ketoacyl-CoA thiolase activity. Genetic loci for both subunits are at 2p23. Medium-chain acyl-CoA dehydrogenase (EC 1.3.99.3, abbr.: MCAD) is a homotetramer present in the mitochondrial matrix and acts on fatty acids of chain length 4 — 12 carbon atoms. Its gene locus is at 1p31. Short-chain acyl-CoA dehydrogenase (butgryl-CoA dehydrogenase, EC1.3.99.2, abbr.: SCAD), also a homotetramer, acts on fatty acids of 4 — 6 carbon atoms chain length. Its locus at 12q22-qter encodes a mature protein of 388 amino acids. Disease-causing mutations are known in all four enzymes.
| acyl-CoA, acyl migration, acyl enzyme | |
| acyl-CoA reductase, acylation, acylglycerol |
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Acyl-CoA dehydrogenase
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Acyl-CoA dehydrogenase (NADP+)
| acyl-CoA dehydrogenase (NADP+) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 1.3.1.8 | ||||||
| CAS number | 37251-07-3 | ||||||
| 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 / EGO | ||||||
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In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction
- acyl-CoA + NADP+
2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ 2-oxidoreductase. Other names in common use include 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide, phosphate), enoyl coenzyme A reductase, crotonyl coenzyme A reductase, crotonyl-CoA reductase, and acyl-CoA dehydrogenase (NADP+).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YXM.
References
- ^ PDB 3HZZ; Scarsdale, J.N., Musayev, F.N., Hazzard, C., Florova, G., Reynolds, K., Wright, H.T. (2010). "Structure of Streptomycs collinus crotonyl COA carboxylase/reductase". To be Published. doi:10.2210/pdb3hzz/pdb. http://www.rcsb.org/pdb/explore/explore.do?structureId=3HZZ.; rendered using PyMOL.
- Dommes V, Luster W, Cvetanovic M, Kunau WH (1982). "Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli". Eur. J. Biochem. 125 (2): 335–41. doi:10.1111/j.1432-1033.1982.tb06688.x. PMID 6749495.
- Seubert W, Lamberts I, Kramer R, Ohly B (1968). "On the mechanism of malonyl-CoA-independent fatty acid synthesis. I The mechanism of elongation of long-chain fatty acids by acetyl-CoA". Biochim. Biophys. Acta. 164 (3): 498–517. PMID 4387390.
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