作者: Angela Stöckel , Beate Stiebitz , Klaus Neubert
DOI: 10.1007/978-1-4757-9613-1_5
关键词:
摘要: Aminopeptidase P (APP, EC 3.4.11.9) is a metal-dependent proline-specific peptidase. The enzyme splits N-terminal Xaa-Pro peptide bonds and plays an important role in the regulation of physiological activity peptides, e. g. bradykinin.1, 2 Only recently, first specific inhibitor APP, apstatin, was discovered.’ It known, however, that peptides containing 2-hydroxy-3-amino acids like bestatin amastatin are inhibitors peptidases leucine aminopeptidase (LAP), B M.4 X-ray crystallografic results demonstrated chelation one active Zinc ions bovine lens LAP.’ Bestatin seems to be natural mimetic tetrahedral intermediat LAP-catalyzed substrate hydrolysis.