Analysis of protein-protein interaction and electron transfer between plant ferredoxin and sulfite reductase by site-directed mutagenesis

1997 ◽  
Vol 67 (1-4) ◽  
pp. 407
Author(s):  
T. Akashi ◽  
T. Ideguchi ◽  
K. Kobayashi ◽  
S. Tagawa ◽  
T. Hase
1998 ◽  
Vol 332 (2) ◽  
pp. 293-296 ◽  
Author(s):  
Peter LEE-ROBICHAUD ◽  
Monika E. AKHTAR ◽  
Muhammad AKHTAR

The lyase activity of human CYP17 (17α-hydroxylase-17,20-lyase also P-450c17 or P-45017α) is greatly dependent on the presence of cytochrome b5, and this effect has been ascribed an important regulatory role [Lee-Robichaud, Wright, Akhtar and Akhtar (1995) Biochem. J. 308, 901–908]. This facet was further investigated by site-directed mutagenesis of selected basic residues of human CYP17. The purified mutant proteins were subjected to detailed kinetic analysis. It was found that the mutation of Lys83, Arg347 and Arg358 produced proteins that were deficient in their responsiveness to cytochrome b5, and the effect was most pronounced for the two arginine mutants (Arg347 → His and Arg358 → Gln) which have been found in male patients suffering from genital ambiguity. These residues are invoked to mediate protein–protein interaction between cytochrome b5 and CYP17, which ‘awakens ’ the lyase activity of the enzyme required for androgen formation.


2002 ◽  
Vol 124 (20) ◽  
pp. 5684-5691 ◽  
Author(s):  
Laura S. Koo ◽  
Chad E. Immoos ◽  
Michael S. Cohen ◽  
Patrick J. Farmer ◽  
Paul R. Ortiz de Montellano

1990 ◽  
Vol 112 (2) ◽  
pp. 907-908 ◽  
Author(s):  
Mart Van de Kamp ◽  
Rene Floris ◽  
Frits C. Hali ◽  
Gerard W. Canters

Biochemistry ◽  
2009 ◽  
Vol 48 (44) ◽  
pp. 10665-10678 ◽  
Author(s):  
Nobuyuki Nakanishi ◽  
Motiur Md. Rahman ◽  
Yoichi Sakamoto ◽  
Tadakazu Takigami ◽  
Kazuo Kobayashi ◽  
...  

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