Bestatin inhibits covalent coupling of [3H]LTA4 to human leukocyte LTA4hydrolase

FEBS Letters

Kargman, Stacia¹  Evans, Jilly F.¹ 

[1] Department of Pharmacology, Merck Frosst Centre for Therapeutic Research, Pointe Claire-Dorval, Quebec, Canada

关键词: LTA4 hydrolase;    Bestatin;    [3H]LTA4 covalent coupling;    Human leukocyte;    LTA3;    5(S)-trans-5;    6-oxido-7;    9-trans-11-cis-eicosatetraenoic acid;    LTA4;    5(S)-trans-5;    6-oxido-7;    9-trans-11;    14-cis-eicosatetraenoic acid;    LTA5;    5(S)-trans-5;    6-oxido-7;    9-trans-11;    14;    17-cis-eicosatetraenoic acid;    LTB4;    5(S);    12(R)-dihydroxy-8;    10-trans-6;    14-cis-eicosatetraenoic acid;   

DOI  :  10.1016/0014-5793(92)80345-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown