Bestatin inhibits covalent coupling of [3H]LTA4 to human leukocyte LTA4 hydrolase.
The covalent coupling of [3H]LTA4 to human leukocyte LTA4 hydrolase is inhibited in a concentration-dependent fashion by pre-incubation with bestatin. This inhibition correlated with the concentration-dependent inhibition by bestatin of LTB4 and LTB5 synthesis by LTA4 hydrolase. Epibestatin, a diastereomer of bestatin, neither inhibited LTB4 or LTB5 production by LTA4 hydrolase nor prevented the covalent coupling of [3H]LTA4 to the enzyme. In contrast, captopril inhibited both LTB4 synthesis by LTA4 hydrolase and covalent coupling of [3H]LTA4 to the enzyme.
Evans
J F
JF
Department of Pharmacology, Merck Frosst Centre for Therapeutic Research, Pointe Claire-Dorval, Quebec, Canada.
Kargman
S
S
D002216:Captopril / Q000494:pharmacology; D002850:Chromatography, Gel; D004851:Epoxide Hydrolases / Q000378:metabolism*; D006801:Humans; D007930:Leucine / Q000031:analogs & derivatives* / Q000494:pharmacology; D007962:Leukocytes / Q000201:enzymology*; D017572:Leukotriene A4; D020024:Leukotriene Antagonists; D007975:Leukotriene B4 / Q000037:antagonists & inhibitors / Q000378:metabolism; D015289:Leukotrienes / Q000378:metabolism*
D017572:Leukotriene A4; D020024:Leukotriene Antagonists; D015289:Leukotrienes; D007975:Leukotriene B4; D002216:Captopril; D004851:Epoxide Hydrolases; D007930:Leucine; C012211:ubenimex; C043134:leukotriene A4 hydrolase