Bestatin inhibits covalent coupling of [3H]LTA4to human leukocyte LTA4hydrolase
- 3 February 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 297 (1-2) , 139-142
- https://doi.org/10.1016/0014-5793(92)80345-h
Abstract
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.Keywords
This publication has 14 references indexed in Scilit:
- Leukotriene A4 hydrolase is a zinc-containing aminopeptidaseBiochemical and Biophysical Research Communications, 1990
- Leukotriene A4 hydrolase: A zinc metalloenzymeBiochemical and Biophysical Research Communications, 1990
- Leukotriene A4 hydrolase: An epoxide hydrolase with peptidase activityBiochemical and Biophysical Research Communications, 1990
- Molecular evolution and zinc ion binding motif of leukotriene A4 hydrolaseBiochemical and Biophysical Research Communications, 1990
- Leukotriene A 5 is a substrate and an inhibitor of rat and human neutrophil LTA 4 hydrolaseBiochemical and Biophysical Research Communications, 1985
- Purification and characterisation of leukotriene A4 hydrolase from rat neutrophilsBiochimica et Biophysica Acta (BBA) - General Subjects, 1985
- Leukotrienes: Mediators of Immediate Hypersensitivity Reactions and InflammationScience, 1983
- Leukotriene B, a potent chemokinetic and aggregating substance released from polymorphonuclear leukocytesNature, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970