The enzymatic profile of Haemophilus ducreyi.
The enzymatic activities of two reference strains of Haemophilus ducreyi and thirty clinical isolates were investigated by conventional biochemical tests and the API-ZYM test kit system which included 97 synthetic substrates. No strains converted delta-aminolevulinic acid to porphyrins, but they all reduced nitrates to nitrites. All strains possessed aminopeptidase activity against beta-naphthylamide derivatives of L-alanine, L-arginine, L-glutamine, glycine, L-leucine, L-lysine and L-serine. No trypsinor chymotrypsin-like activities were detected. All strains had phosphatase activity with broad pH range, and phosphoamidase activity. No glycosidase was detected by the substrates tested.
D000626:Aminopeptidases / Q000378:metabolism; D004950:Esterases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006191:Haemophilus ducreyi / Q000201:enzymology*; D006867:Hydrolases / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism
D006867:Hydrolases; D004950:Esterases; D010744:Phosphoric Monoester Hydrolases; D006026:Glycoside Hydrolases; D010447:Peptide Hydrolases; D000626:Aminopeptidases