Identification and characterisation of two extracellular proteases of Streptococcus mutans.
Streptococcus mutans was shown to produce two extracellular proteases capable of degrading both gelatin and collagen-like substrates. These enzymes have molecular masses of 52 and 50 kDa when analysed by SDS-PAGE. Both enzymes were inhibited by EDTA, but not by a range of other inhibitors with different specificities, indicating that they are metalloproteases. The activity of EDTA-inactivated enzymes could be restored by the addition of manganese and zinc. The identical inhibition and restoration profiles of the two enzymes suggest that one of the proteases may be a degradation product of the other.
Harrington
D J
DJ
Department of Oral Biology, Dental School, University of Newcastle upon Tyne, UK.
Russell
R R
RR
D002850:Chromatography, Gel; D003094:Collagen / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D005780:Gelatin / Q000378:metabolism; D013291:Streptococcus / Q000201:enzymology*
D005780:Gelatin; D003094:Collagen; D010450:Endopeptidases