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- W2952751331 abstract "Amastatin [(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-L-valyl-L-valyl-L- aspartic acid] and bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine] are slow-binding, competitive inhibitors of aminopeptidase M (AP-M) with net inhibition constants (Ki) of 1.9 X 10(-8) and 4.1 X 10(-6) M, respectively. The effect of inhibitor structure on net Ki and on slow-binding inhibition was evaluated for analogues of both inhibitors on AP-M and leucine aminopeptidase (LAP). The (2S)-hydroxyl group contributes to the stabilization of a collision complex [EI], which is formed rapidly. In contrast, increasing the peptide chain length of the inhibitor produces more potent inhibitors as a consequence of a slower binding process. A statine analogue of amastatin [(3S,4S)-Sta-Val-Val-Asp] stimulated rather than inhibited LAP. AP-M binds tri- and tetrapeptide inhibitors more strongly than dipeptide inhibitors, whereas LAP binds dipeptide inhibitors more strongly. The difference in binding can be used to distinguish cytosolic from membrane-bound aminopeptidases." @default.
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- W2952751331 date "1984-09-18" @default.
- W2952751331 modified "2023-09-23" @default.
- W2952751331 title "ChemInform Abstract: INHIBITION OF AMINOPEPTIDASES BY AMASTATIN AND BESTATIN DERIVATIVES. EFFECT OF INHIBITOR STRUCTURE ON SLOW-BINDING PROCESSES" @default.
- W2952751331 cites W2024507420 @default.
- W2952751331 doi "https://doi.org/10.1002/chin.198438323" @default.
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