Bovine‐Lens Leucine Aminopeptidase
作者： Siegfried Fittkau , Ulrike Forster , Wolf-Hagen Schunck , Carlos Pascual
DOI: 10.1111/J.1432-1033.1974.TB03511.X
关键词:
摘要: The inhibition of leucine aminopeptidase isolated from bovine eye lens by the chloromethyl ketones l-phenylalanine (PheCH2Cl) and l-leucine (LeuCH2Cl) has been studied. these substances is rather strong. Their action shown to be reversible competitive with an constant order K1 0.1 mM. N-Methylated inhibitors substrates have a lower affinity, N-acylated derivatives normal do not act as inhibitors. The tripeptide Thr(OBut)-Phe-Pro hydrazide substrate, K1= 0.02 mM, agrees other values which obtained using 4-nitro-anilide substrate. A model for binding step in active center developed calculated free energy ΔG0 methyl or N-methylated α-amino group Km their analogous amino acid hydrazides. These follows. 1 The hydrophobic residues amino-acid hydrazides amides causes “one-site” bonding enzyme. 2 As case ketones, peptides affinity increases additional C-terminal part. It results “three-site” peptide substrates. 3 The complexation substrate inhibitor preliminary condition towards hydro-phobic binding. Therefore sterically attainable basic function unprotonated form necessary. The discussed compared kinetic data literature.
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