Arylamidase activity of Salmonella species.
Arylamidase activity in cell extracts of sonically cell treated suspensions of 23 Salmonella strains, including 12 strains of S. typhimurium, was investigated. All cultures hydrolyzed five of nine different neutral and basic substrates. Activity against aspartyl-, cystyl- histidinyl-, and isoleucyl-beta-naphylamide was negligible. Alanyl-beta-naphthylamide was the preferred substrate for the Salmonella species; however, specific activities ranged widely. Of several gram-negative organisms surveyed, all except Proteus vulgaris hydrolyzed alanyl-beta-naphthylamide at the fastest rate. The most preferred substrate for the Proteus culture was glycyl-beta-naphthylamide. No relationship could be shown between virulence and arylamidase activity for the Salmonella strains.
D000577:Amides / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism*; D002474:Cell-Free System; D004926:Escherichia coli / Q000201:enzymology; D009281:Naphthalenes / Q000378:metabolism; D011514:Proteus vulgaris / Q000201:enzymology; D011551:Pseudomonas fluorescens / Q000201:enzymology; D012475:Salmonella / Q000201:enzymology* / Q000472:pathogenicity; D012486:Salmonella typhimurium / Q000201:enzymology / Q000472:pathogenicity; D012706:Serratia marcescens / Q000201:enzymology; D012763:Shigella flexneri / Q000201:enzymology; D013010:Sonication; D013045:Species Specificity; D014774:Virulence
D000577:Amides; D000596:Amino Acids; D009281:Naphthalenes; D000626:Aminopeptidases