Acil-KoA dehidrogenaza (NADP+)
Izgled
Acil-KoA dehidrogenaza (NADP+) | |||||||||
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Acil-KoA dehidrogenaza (NADP+) tetramer, Human | |||||||||
Identifikatori | |||||||||
EC broj | 1.3.1.8 | ||||||||
CAS broj | 37251-07-3 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Acil-KoA dehidrogenaza (NADP+) (EC 1.3.1.8, 2-enoil-KoA reduktaza, dehidrogenaza, acil koenzim A (nikotinamid adenin dinukleotid fosfat), enoil koenzim A reduktaza, krotonil koenzim A reduktaza, krotonil-KoA reduktaza) je enzim sa sistematskim imenom acil-KoA:NADP+ 2-oksidoreduktaza.[1][2] Ovaj enzim katalizuje sledeću hemijsku reakciju
- acil-KoA + NADP+ 2,3-dehidroacil-KoA + NADPH + H+
Ovaj jetreni enzim deluje na enoil-KoA derivate sa ugljeničnim lancom dugim 4 do 16 atoma, sa optimalnom aktivnošću na 2-heksenoil-KoA. kod Escherichia coli, postoji cis-specifični i trans-specifični enzim (EC 1.3.1.37, cis-2-enoil-KoA reduktaza (NADPH) i EC 1.3.1.38, trans-2-enoil-KoA reduktaza (NADPH)).
- ↑ Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. (1982). „Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli”. Eur. J. Biochem. 125: 335-341. PMID 6749495.
- ↑ Seubert, W., Lamberts, I., Kramer, R. and 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: 498-517. PMID 4387390.
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