Article
Leukotriene A4 hydrolase: a critical role of glutamic acid-296 for the binding of bestatin.
The Biochemical journal - 1 Feb 2000
Andberg M, Wetterholm A, Medina J F, Haeggström J Z
Abstract excerpt
Leukotriene A(4) hydrolase is a bifunctional Zn(2+)-containing enzyme catalysing the formation of the potent chemotaxin leukotriene B(4). From an analysis of three mutants of Glu-296 we have found that this catalytic residue is critical for the binding of bestatin, a classical aminopeptidase inhibitor. For bestatin, but not for three other tight-binding inhibitors, the IC(50) values for inhibition of the epoxide...
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