Enzymatic profile of Legionella pneumophilia.
The enzyme activities of four strains of Legionella pneumophilia were investigated by using the API ZYM system (API System S.A., F-38390 Montalieu Vercieu, France) and synthetic substrates. Aminopeptidases were detected specifically against L-alanine, L-arginine, L-aspartic acid, L-cystine, L-glutaminic acid, glycine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-tryptophan, L-tyrosine, and L-valine. Furthermore, the bacteria possesses esterase activity splitting propionate, butyrate, caproate, caprylate, and caprate, but not laurate, myristate, palmitate, and stearate, esters. The enzymes studies were inhibited partially by aprotinin. No inhibition of phosphatase (pH range, 5.4 to 8.5) or of phosphoamidase was observed. Activities of arylsulfatase, chymotrypsin, trypsin, and glycosidases could not be detected.
D000626:Aminopeptidases / Q000378:metabolism; D007611:Aprotinin / Q000494:pharmacology; D004950:Esterases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D007875:Legionella / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism; D013429:Sulfatases / Q000378:metabolism
D007611:Aprotinin; D006867:Hydrolases; D004950:Esterases; D013429:Sulfatases; D006026:Glycoside Hydrolases; D010447:Peptide Hydrolases; D000626:Aminopeptidases