6533b7d0fe1ef96bd125a174

RESEARCH PRODUCT

Cell Surface-Bound Leucine Aminopeptidase: Target of the Immunomodulator Bestatin

subject

description

The study of low molecular weight enzyme inhibitors of microbial origin was initiated by Umezawa in 1965 (see Umezawa 1972). Since the discovery of an inhibitor of tyrosine hydroxylase, nearly 50 inhibitors of various enzymes have been found by him; their structures were elucidated and most of the compounds were chemically synthesized (Umezawa 1982). Among them one inhibitor of both aminopeptidase B and the ectoenzyme, leucine aminopeptidase was found in 1976 and was termed bestatin (Fig. 1), [(2S,3R)-3-amino-2-hydroxy 4-phenyl-butanoyl]-(S)-leucine (Umezawa et al. 1976).