Indication of thioglucosidase activity in extracts of Neisseria gonorrhoeae.
The recent demonstration of a host-derived inducer of gonococcal resistance to complement-mediated killing by human serum in purified serum and red blood cell fractions, which contained small glucopeptides with cysteine as one of the constituent amino acids, prompted an investigation of Neisseria gonorrhoeae for thioglucosidase activity. This involved an examination of supernatants of sonicated gonococci for thioglucoside hydrolysis by following, spectroscopically, the hydrolysis of 6-purine beta-D-glucothiopyranoside to 6-mercaptopurine and glucose. Extracts of N. gonorrhoeae were found to hydrolyse this thioglucoside. A substantial activity was present in a fraction with the same order of molecular weight as plant thioglucosidases. This led us to suspect the presence of a thioglucosidase in N. gonorrhoeae.
D006026:Glycoside Hydrolases / Q000032:analysis* / Q000378:metabolism; D006868:Hydrolysis; D008970:Molecular Weight; D009344:Neisseria gonorrhoeae / Q000201:enzymology*; D014462:Ultrafiltration
D006026:Glycoside Hydrolases; C022739:thioglucosidase