Site-Directed Mutagenesis Reveals Critical Importance of the Catalytic Site in the Binding of .alpha.-Amylase by Wheat Proteinaceous Inhibitor

Biochemistry ◽  
1994 ◽  
Vol 33 (25) ◽  
pp. 7925-7930 ◽  
Author(s):  
Kenji Takase
FEBS Letters ◽  
1998 ◽  
Vol 435 (1) ◽  
pp. 16-20 ◽  
Author(s):  
Jinq-May Chen ◽  
Richard A.E. Stevens ◽  
Paul W. Wray ◽  
Neil D. Rawlings ◽  
Alan J. Barrett

Biochemistry ◽  
1992 ◽  
Vol 31 (22) ◽  
pp. 5232-5236 ◽  
Author(s):  
Ikuo Matsui ◽  
Kazuhiko Ishikawa ◽  
Sachio Miyairi ◽  
Sakuzo Fukui ◽  
Koichi Honda

FEBS Letters ◽  
1988 ◽  
Vol 231 (1) ◽  
pp. 54-58 ◽  
Author(s):  
Alain Devault ◽  
Valérie Sales ◽  
Christiane Nault ◽  
Ann Beaumont ◽  
Bernard Roques ◽  
...  

1997 ◽  
Vol 43 (8) ◽  
pp. 792-795 ◽  
Author(s):  
Celestino Di Flumeri ◽  
Nicholas H. Acheson ◽  
Teresa Keng

Uroporphyrinogen decarboxylase catalyzes the fifth step of heme biosynthesis in Saccharomyces cerevisiae. Studies utilizing sulfhydryl-specific reagents suggest that the enzyme requires a cysteine residue within the catalytic site This hypothesis was tested directly by site-directed mutagenesis of highly conserved cysteine-52 to serine or alanine. Plasmids containing these mutations were able to complement a hem6 mutant strain. In addition, properties associated with decreased uroporphyrinogen decarboxylase activity were not detected in the mutant strain transformed with these mutant plasmids. These results suggest that the conserved cysteine-52 by itself is not essential for enzymatic activity.Key words: heme biosynthesis, uroporphyrinogen decarboxylase, site-directed mutagenesis.


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