Sialidase-like enzymes produced by group A, B, C, G, and L streptococci and by Streptococcus sanguis.
A group of enzymes were prepared from the culture fluids of streptococci belonging to groups A, B, C, G, and L, and from a strain of Streptococcus sanguis. These streptococcal enzymes (designated St-sialidases) released a substance shown to belong to the sialic acid group from the specific substrate BSM-St, a sialomucoid prepared from bovine submaxillary gland. They were inactive on N-acetylneuramin lactose prepared from bovine colustrum and on a sialomucoid prepared from bovine submaxillary mucin, whereas these substances are susceptible to sialidases produced by group K streptococci and by Vibrio cholerae. Some of the St-sialidases were markedly activated by divalent cations, but others showed little response. The heat stability of the enzymes produced by the different strains varied. The optimal pH was between 5.5 and 6.5 with acetate buffer and was about 7 with phosphate buffer. K(m) values were determined for the St-sialidases with BSM-St as substrate.
D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D009077:Mucins / Q000378:metabolism; D009438:Neuraminic Acids / Q000378:metabolism; D009439:Neuraminidase / Q000302:isolation & purification; D013053:Spectrophotometry; D013291:Streptococcus / Q000201:enzymology*
D008670:Metals; D009077:Mucins; D009438:Neuraminic Acids; D009439:Neuraminidase