Structural highlights
Function
[NCPR2_ARATH] This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and dichloroindophenol.[HAMAP-Rule:MF_03212][1] [2] [3] [4] [5]
References
- ↑ Hull AK, Celenza JL. Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2. Protein Expr Purif. 2000 Apr;18(3):310-5. PMID:10733884 doi:http://dx.doi.org/10.1006/prep.1999.1195
- ↑ Urban P, Mignotte C, Kazmaier M, Delorme F, Pompon D. Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5. J Biol Chem. 1997 Aug 1;272(31):19176-86. PMID:9235908
- ↑ Mizutani M, Ohta D. Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation. Plant Physiol. 1998 Jan;116(1):357-67. PMID:9449848
- ↑ Fukuchi-Mizutani M, Mizutani M, Tanaka Y, Kusumi T, Ohta D. Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis. Plant Physiol. 1999 Jan;119(1):353-62. PMID:9880378
- ↑ Louerat-Oriou B, Perret A, Pompon D. Differential redox and electron-transfer properties of purified yeast, plant and human NADPH-cytochrome P-450 reductases highly modulate cytochrome P-450 activities. Eur J Biochem. 1998 Dec 15;258(3):1040-9. PMID:9990323