A strong competitive peptide-inhibitor for leucine aminopeptidase
نویسندگان
چکیده
منابع مشابه
Leucine Aminopeptidase (Bovine Lens)
The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,...
متن کاملLeucine Aminopeptidase (Bovine Lens)
Spark emission and atomic absorption spectroscopy of crystalline leucine aminopeptidase (bovine lens) (EC 3.4.1.1) shows the presence of 2 zinc atoms per subunit molecular weight of 54,000 (12 zinc atoms per oligomer of 320,000). Removal of zinc by dialysis yields a zinc-free product with no enzymatic activity which upon readdition of Zn2+, regains full activity with the concomitant binding of ...
متن کاملLeucine Aminopeptidase (Bovine Lens)
The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,...
متن کاملLeucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis.
The three-dimensional structures of native bovine lens leucine aminopeptidase (EC 3.4.11.1) and its complex with bestatin, a slow-binding inhibitor, have been solved and exhaustively refined. The mode of binding of bestatin to leucine aminopeptidase may be similar to that of a tetrahedral intermediate that is thought to form during peptide bond hydrolysis. Bestatin binds in the active site with...
متن کاملThe specificity of leucine aminopeptidase.
Since Linderstr@m-Lang’s demonstration that the hydrolysis of Lleucylglycine (LG) is due to a distinctileucyl peptidase (l), various studies have shown that this enzyme is widely distributed (24) and requires for its activity the presence of Mn++ or Mg++ ions (2, 5). The enzyme has been regarded as a typical aminopeptidase (5), since it does not hydrolyze acylated compounds Such as benzoyl-L-le...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1972
ISSN: 0014-5793
DOI: 10.1016/0014-5793(72)80343-0