Isolation purification and properties of a site-specific proteolytic enzyme "valyl-proteinase" from Candida tropicalis.
A highly specific proteolytic enzyme cleaving at the carboxyl group of valine has been isolated from Candida tropicalis. Its specificity has been determined by digesting beta-lactoglobulin and a number of synthetic peptides. The enzyme a glycoprotein, has a molecular mass of 40 +/- 7 kDa on the basis of sodium dodecyl sulphate polyacrylamide gel electrophoresis. Its optimum activity occurs at 37 degrees C at a pH between 8-9. It has been named "Valyl-proteinase" because of its selective cleavage.
D000596:Amino Acids / Q000032:analysis; D002175:Candida / Q000201:enzymology*; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006023:Glycoproteins / Q000302:isolation & purification; D006601:Hexoses / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D014633:Valine
D000596:Amino Acids; D006023:Glycoproteins; D006601:Hexoses; D010450:Endopeptidases; D010447:Peptide Hydrolases; C049656:valyl proteinase; D014633:Valine