Comparison of peptidase, glycosidase and esterase activities of oral and non-oral Treponema species.
The enzyme profiles of 20 oral and non-oral Treponema strains were investigated using an API ZYM Complete Research kit. The test included 10 2-naphthyl derivatives of fatty acids, 20 p-nitrophenol derivatives of carbohydrates and 60 2-naphthylamide derivatives of amino acids and peptides. The oral Treponema species investigated were T. denticola, T. vincentii and T. Pectinovorum. The non-oral species examined were T. phagedenis, T. hyodysenteriae and intestinal spirochaetes of human and chicken origin. Esterase activities on C5 to C10 fatty acids were common among different Treponema species. Glycosidase activities were infrequently observed in T. vincentii, T. pectinovorum and T. phagedenis Reiter strain. Arabinosidase, lactosidase and xylosidase activity was observed in the T. hyodysenteriae strains but alpha-L-fucosidase activity was found only in T. denticola and T. phagedenis. More exo- and endo-peptidase activities were found in T. denticola than in other species. The enteropathogenic T. hyodysenteriae isolates had a very low proteolytic profile. Dipeptidyl prolyl amidase activity was observed in all species except in the T. phagedenis Reiter strain and the avian intestinal spirochaetes. The enzyme profiles did not discriminate between oral and non-oral Treponema species.
Mikx
F H
FH
Department of Periodontology and Preventive Dentistry, University of Nijmegen, The Netherlands.
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D001717:Birds; D010450:Endopeptidases / Q000378:metabolism*; D004950:Esterases / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D014208:Treponema / Q000201:enzymology*
D004950:Esterases; D006026:Glycoside Hydrolases; D010450:Endopeptidases; D000626:Aminopeptidases