Premium
L‐Leucyl‐sarkosyl‐L‐phenylalanin, Synthese und Wirkung auf die Aminopeptidasen I und II von Bacillus stearothermophilus
Author(s) -
Jost Rolf,
TunKyi Aung,
Stoll Erwin,
Zuber Herbert
Publication year - 1972
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19720550327
Subject(s) - chemistry , dipeptide , tripeptide , phenylalanine , hydrolysis , stereochemistry , leucine , enzyme , substrate (aquarium) , peptide , biochemistry , amino acid , geology , oceanography
The synthesis of L‐leucyl‐sarcosyl‐L‐phenylalanine is described. This tripeptide resists hydrolysis by the aminopeptidases AP I and AP II from Bacillus stearothermophilus . The peptide is a reversible inhibitor of both enzymes. The inhibition constant for AP I is 5 × 10 −3 mol/l and 1.5 × 10 −3 mol/l for AP II. In the hydrolysis of leucine p‐nitroanilide we observed noncompetitive inhibition by leucylsarcosyl‐phenylalanine with both enzymes. With dipeptide substrates however, the inhibitory effect of leucyl‐sarcosyl‐phenylalanine was drastically reduced by saturating substrate concentrations.