βD305A Mutant of Tryptophan Synthase Shows Strongly Perturbed Allosteric Regulation and Substrate Specificity†

Biochemistry ◽  
2001 ◽  
Vol 40 (25) ◽  
pp. 7421-7432 ◽  
Author(s):  
Davide Ferrari ◽  
Li-Hong Yang ◽  
Edith W. Miles ◽  
Michael F. Dunn
1990 ◽  
Vol 63 (8) ◽  
pp. 2339-2345 ◽  
Author(s):  
Yukito Murakami ◽  
Jun-ichi Kikuchi ◽  
Yoshio Hisaeda ◽  
Koichiro Nakamura ◽  
Tomoyuki Kitazaki ◽  
...  

Biochemistry ◽  
2007 ◽  
Vol 46 (26) ◽  
pp. 7728-7739 ◽  
Author(s):  
Patricia Casino ◽  
Dimitri Niks ◽  
Huu Ngo ◽  
Peng Pan ◽  
Peter Brzovic ◽  
...  

2002 ◽  
Vol 324 (4) ◽  
pp. 677-690 ◽  
Author(s):  
Victor Kulik ◽  
Michael Weyand ◽  
Ralf Seidel ◽  
Dimitri Niks ◽  
Demet Arac ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (15) ◽  
pp. 3374
Author(s):  
Adam R. Offenbacher ◽  
Theodore R. Holman

Lipoxygenases (LOXs) catalyze the (per) oxidation of fatty acids that serve as important mediators for cell signaling and inflammation. These reactions are initiated by a C-H activation step that is allosterically regulated in plant and animal enzymes. LOXs from higher eukaryotes are equipped with an N-terminal PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain that has been implicated to bind to small molecule allosteric effectors, which in turn modulate substrate specificity and the rate-limiting steps of catalysis. Herein, the kinetic and structural evidence that describes the allosteric regulation of plant and animal lipoxygenase chemistry by fatty acids and their derivatives are summarized.


Biochemistry ◽  
2016 ◽  
Vol 55 (51) ◽  
pp. 7043-7046 ◽  
Author(s):  
Andrew R. Buller ◽  
Paul van Roye ◽  
Javier Murciano-Calles ◽  
Frances H. Arnold

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