PepCs isolated from lactic acid bacteria and bleomycin hydrolases of eukaryotic organisms are strict aminopeptidases which belong to the papain family of thiol peptidases. The structural basis of the enzymic specificity of the lactococcal PepC has been investigated by site-directed mutagenesis. The deletion of the C-terminal residue (Ala-435) abolished the aminopeptidase activity, whereas this ...

In this paper, the authors use the logistic temporal solution of the generalized Michaelis-Menten kinetics to provide a quantum basis for the tunnelling time and energy evaluations of Brownian enzymic reactions. The mono-substrate and mixed inhibition cases are treated and the associated quantum diagrams of the reaction mechanisms are depicted in terms of intermediate enzyme complexes. The meth...

Studies of the chemical properties of the enzyme, catecholase, have shown that this polyphenoloxidase consists of a copper-protein complex (l-3). Indications have also been obtained that the enzymic activity of catecholase is associated with the copper part of the molecule, since it has been found that the addition of certain reagents known to react with cupric ions will inhibit the enzymic act...

The lipid lowering activity of Anthocephalus indicus (family Rubiaceae; Hindi name Kadamba) root extract has been studied in triton WR-1339 induced hyperlipidemia in rats. In this model, feeding with root extract (500 mg kg(-1) b.w.) lowered plasma lipids and reactivated post-heparin lipolytic activity in hyperlipidemic rats. Furthermore, the root extract (50-500 μM) inhibited the generation of...

1. The sensitivity of the NAD(+)-specific isocitrate dehydrogenase from baker's yeast towards inhibition by anions decreases with decrease in pH. The patterns of the pH-dependence of the enzymic activity can be explained by this effect. 2. In the presence of a high isocitrate concentration, citrate, unlike AMP, has no antagonizing effect on the inhibition of the enzyme by anions. In the presenc...