[Investigations of the enzyme spectrum of Erysipelothrix rhusiopathiae (author's transl)].
The enzyme spectrum of non proliferating cells of Erysipelothrix rhusiopathiae was investigated by means of different low molecular synthetic substrates. Activities of aminopeptidases were found directed against compounds of L-alanine, L-arginine, L-aspartic acid, glycine, L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-proline, L-tryptophane, and L-tyrosine, but not against compounds of l-cystine, L-glutaminic acid, L-histidine, L-hydroxyproline, and L-valine (Table 1). The pH optimum of the investigated aminopeptidases ranges from neutral to alkaline reaction (Table 2). Trypsin, chymotrypsin, or chymotrypsin-like proteases were not detected. E. rhusiopathiae possess esterase activity splitting esters of lower carboxylic acids, i. e. acetic acid, propionic acid, butyric acid, caproic acid, and caprylic acid, but no lipase activity. Under the provoked glycosidases only alpha- and beta-D-galactosidase and glucosaminidase were positive. Weak activities of phosphatases and arylsulfatase were found also (Table 3).
D000626:Aminopeptidases / Q000378:metabolism*; D001192:Arylsulfatases / Q000378:metabolism; D004888:Erysipelothrix / Q000201:enzymology*; D004950:Esterases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism
D006867:Hydrolases; D004950:Esterases; D010744:Phosphoric Monoester Hydrolases; D001192:Arylsulfatases; D006026:Glycoside Hydrolases; D010447:Peptide Hydrolases; D000626:Aminopeptidases
Untersuchungen zum Enzymspektrum von Erysipelothrix rhusiopathiiase.