Complete amino acid sequence of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes

Biochemistry ◽  
1986 ◽  
Vol 25 (24) ◽  
pp. 7906-7911 ◽  
Author(s):  
Mitsuru Haniu ◽  
Takashi Iyanagi ◽  
Philip Miller ◽  
Terry D. Lee ◽  
John E. Shively
1986 ◽  
Vol 236 (3) ◽  
pp. 871-878 ◽  
Author(s):  
F Vogel ◽  
L Lumper

The 622-residue amino acid sequence of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase (EC 1.6.2.4) is reported. The structural data required to complete the sequences published previously [Vogel, Kaiser, Witt & Lumper (1985) Biol. Chem. Hoppe-Seyler 366, 577-587] and to establish the primary structure of the porcine hydrophilic domain have been obtained by sequencing proteolytic subfragments derived from CNBr fragments and by characterizing the overlapping S-[14C]methylmethionine-containing peptides isolated from tryptic digests of the [14C]methyl-labelled hydrophilic domain. The hydrophilic domain displays 91.8% positional identity with that of the corresponding domain in the rat NADPH-cytochrome P-450 reductase. The region Val528-Ser678 in the NADPH-cytochrome P-450 reductase shows a significant homology to the sequence Ile165-Tyr314 in the spinach ferredoxin-NADP+ oxidoreductase. A model for the secondary structure of the hydrophilic domain has been derived by computer-assisted analysis of the amino acid sequence. Cys472 and Cys566 are protected against chemical modification in the NADP+ complex of the NADPH-cytochrome P-450 reductase.


1987 ◽  
Vol 254 (1) ◽  
pp. 380-384 ◽  
Author(s):  
Mitsuru Haniu ◽  
Kazutoshi Yanagibashi ◽  
Peter F. Hall ◽  
John E. Shively

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  

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