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1.6.2.4: NADPH-hemoprotein reductase

This is an abbreviated version!
For detailed information about NADPH-hemoprotein reductase, go to the full flat file.

Word Map on EC 1.6.2.4

Reaction

NADPH
+
oxidized hemoprotein
=
NADP+
 +
reduced hemoprotein
 +
H+

Synonyms

107366505, aldehyde reductase (NADPH-dependent), ATR2, CPR, CPR I, CPR-X1, CPR-X2, CPR1, CPR2, CYPOR, cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent), cytochrome P450 NADPH reductase, cytochrome P450 oxidoreductase, cytochrome P450 reductase, cytochrome P450-diflavin reductase, dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase, FAD-cytochrome c reductase, ferrihemprotein P450 reductase, flavocytochrome P450 BM3, NAD(P)H cytochrome P450 reductase, NADP-cytochrome c reductase, NADP-cytochrome P-450 reductase, NADP-cytochrome reductase, NADPH cytochrome P450 reductase, NADPH dependent cytochrome P450 reductase, NADPH P450 oxidoreductase, NADPH P450 reductase, NADPH-CPR, NADPH-CYP reductase, NADPH-CYP450 reductase, NADPH-cytochrome c oxidoreductase, NADPH-cytochrome c reductase, NADPH-cytochrome p-450 reductase, NADPH-cytochrome P450 (CYP) oxidoreductase, NADPH-cytochrome P450 oxidoreductase, NADPH-cytochrome P450 reductase, NADPH-cytochrome P450 reductase 2, NADPH-dependent cytochrome c reductase, NADPH-dependent cytochrome P450 reductase, NADPH-dependent P450 reductase, NADPH-ferricytochrome c oxidoreductase, NADPH-ferrihemoprotein reductase, NADPH-P450 reductase, NADPH: cytochrome P450 oxidoreductase, NADPH: cytochrome P450 reductase, NADPH:CYP oxidoreductase, NADPH:cytochrome P450 oxidoreductase, NADPH:cytochrome P450 reductase, NADPH:ferrihemoprotein oxidoreductase, NCP1, neotetrazolin reductase, NPR, NP_000932, P-450 reductase, P450 BM3, P450 oxidoreductase, P450 Red, P450 reductase, P450R, P450REd, POR, RedA, reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase, reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate), SbCPR2, TcCPR-A, TcCPR-B, TcCPR-C, TPNH-cytochrome c reductase, TPNH2 cytochrome c reductase, WsCPR1, WsCPR2

ECTree

     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.2 With a heme protein as acceptor
                1.6.2.4 NADPH-hemoprotein reductase

Crystallization

Crystallization on EC 1.6.2.4 - NADPH-hemoprotein reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 21% (w/v) polyethylene glycol monomethyl ether 2000 and 0.1 M MES, pH 6.5
-
structure of mutant DELTAD675/DELTAV676, the overall protein fold of the mutant structure is the same as the wild-type structure
sitting-drop technique, 4°C, A264Q crystals are obtained with a mother liquor of 100 mM cacodylic acid (pH 6.0), 160 mM MgCl2 and 16% PEG 3350. A264M crystals are obtained with mother liquor of 100 mM cacodylic acid (pH 6.0), 140 mM MgCl2 and 18% PEG 3350. A264C crystals are obtained under the same conditions, but with 100 mM MgCl2. Crystals are flash-frozen in liquid nitrogen using 10% PEG 200 as cryoprotectant. Crystal structures of the mutant haem domains demonstrate axial ligation of P450 haem iron by methionine and glutamine ligands trans to the cysteine thiolate, creating novel haem iron ligand sets in the A264M/Q variants
deletion mutants
purified mutant CYPOR with an engineered disulfide bond between the FAD and FMN domains, with or without complexed NADP+, hanging drop vapour diffusion method, mixing of 0.002 ml of 15 mg/ml protein solution with 0.002 ml of reservoir solution containing 100 mM HEPES, pH 7.2, 150 mM MgCl2, and 17% PEG 335, purified protein is treated with 2 and 20 times molar excess of FMN and NADP+, respectively, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
crystal structure of truncated yeast NADPH-cytochrome P450 reductase, which is functionally active toward its physiological substrate cytochrome P450
-
Saccharomyces cerevisiae /Homo sapiens
modeling of a complex of the FMN domain with cytochrome P450 monooxygenase Tri11. The complex shows significant interface contacts and structural changes on interaction, the hydrogen bonding interactions are observed between Tri11 protein residues R91, R97, K127, P131,K136, Q139, E275, K375, R411, W412, E415, A416, K417, T418, N419, S421, S422, P423, W424, Y425, N426, D427, R428, R429, N436, V437, G438, R440, N441, R445 and CPR FMN domain residues D132, E102, E78, Y70, S82, R83, E202, E208, T96, N169, Y172, T171, G203, A204, T74, Q73, Y125, E127, E173, G128, E129, T131, S177, T76, A77, G75, A123, D100, N133, S72
-