Catalytic and regulatory properties of the Triton and trypsin forms of the brush border hydrolases.
Amphipathic enzymes, invertase (EC 3.2.1.26), 8-amylase (EC 3.2.1.3), and alkaline phosphatase (EC 3.1.3.1), were purified from the rat small intestinal mucosa as trypsin and Triton forms, the catalytic and regulatory characteristics of which were compared in rats and in drosophila. Differences in the catalytic propertiis of the two enzyme forms were demonstrated, which suggested that the hydrophobic part of the enzyme was involved in maintaining optimal conformation of the catalytic part. Many modifiers have beenfound to influence the Triton rather than the trypsin form of the enzyme. It is therefore suggested that the hydrophobic sub-units of the enzymes might be involved in transmitting information from the cytoplasm into the external surface of the membrane, the cell in this way regulating the activity of surface enzymes. If this is indeed the case, it is suggested that the hydrophobic part performs functions not only of external but also of internal regulation.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000681:Amylases / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology*; D004331:Drosophila melanogaster; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000201:enzymology / Q000648:ultrastructure; D007700:Kinetics; D008871:Microvilli / Q000201:enzymology*; D011092:Polyethylene Glycols; D051381:Rats; D013393:Sucrase / Q000378:metabolism; D014357:Trypsin
D011092:Polyethylene Glycols; D006867:Hydrolases; D000469:Alkaline Phosphatase; D000681:Amylases; D013393:Sucrase; D014357:Trypsin