ABSTRACT
Fifteen amino acids were used to investigate their effects on the pig muscle enolase. The basic and hydrophobic amino acids decreased the enzyme activity slightly. In the presence of acidic amino acids such as aspartic and glutamic acid the degree of inhibition was higher. One of the most potent inhibitors was cysteine. The presence of amino acids does not change the affinity to the substrate of enolase 2-phosphoglycerate. The possible physiological influence of amino acids on the function of enolase is discussed.
Subject(s)
Amino Acids/pharmacology , Muscles/enzymology , Phosphopyruvate Hydratase/drug effects , Animals , Phosphopyruvate Hydratase/antagonists & inhibitors , SwineABSTRACT
The treatment of enolase from pig and carp (Cyprinus carpio) with proteases resulted in a decrease of enzymatic activity, which depended on the kind of protease used. The most active were trypsin and subtilisin. Substrate and magnesium ions protected enolase against inactivation. The enolase from pig muscle was much more resistant to protease action than this enzyme from carp muscle. Some differences in the structure between the two enolases are suggested.
Subject(s)
Endopeptidases/pharmacology , Muscles/enzymology , Phosphopyruvate Hydratase/metabolism , Animals , Carps , Enzyme Activation/drug effects , Kinetics , Magnesium/pharmacology , Muscles/drug effects , Phosphopyruvate Hydratase/chemistry , Phosphopyruvate Hydratase/drug effects , Substrate Specificity , SwineABSTRACT
Fourteen carbohydrate metabolites and related compounds were used to investigate the inhibition of enolase from pig muscle. Glucose and fructose decreased the activity very slightly. The degree of inhibition by phosphate derivative was stronger and dependent on the position of phosphate residue. One of the strongest inhibitor was glyceraldehyde-3-phosphate. The presence of inhibitors do not change the affinity to the substrate - 2-phosphoglycerate. The possible physiological role of enolase in carbohydrate metabolism is discussed.
