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Bestatin inhibits covalent coupling of [ 3 H]LTA 4 to human leukocyte LTA 4 hydrolase
Author(s) -
Evans Jilly F.,
Kargman Stacia
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80345-h
Subject(s) - covalent bond , chemistry , hydrolase , enzyme , diastereomer , stereochemistry , biochemistry , organic chemistry
The covalent coupling of [ 3 H]LTA 4 to human leukocyte LTA 4 hydrolase is inhibited in a concentration‐dependent fashion by pre‐incubation with bestatin. This inhibition correlated with the concentration‐dependent inhibition by bestatin of LTB 4 and LTB 5 synthesis by LTA 4 hydrolase. Epibestatin, a diastereomer of bestatin, neither inhibited LTB 4 or LTB 5 production by LTA 4 hydrolase nor prevented the covalent coupling of [ 3 H]LTA 4 to the enzyme. In contrast, captopril inhibited both LTB 4 synthesis by LTA 4 hydrolase and covalent coupling of [ 3 H]LTA 4 to the enzyme.