Characteristics of M-GTFI, a new inhibitor of Streptococcus mutans glucosyltransferase.
M-GTFI, originally screened as an inhibitor of Streptococcus mutans glucosyltransferase, strongly inhibited alpha-glucosidase, in a non-competitive manner especially when the synthetic substrate p-nitrophenyl-alpha-D-glucopyranoside was used. It also inhibited beta-glucosidase, beta-amylase and, to a lesser extent, beta-glucuronidase. The inhibitor was stable in neutral and alkaline pH ranges and dependency of the inhibition on pH and temperature was not observed. Some proteinases and polysaccharides-hydrolyzing enzymes as well as human saliva did not inactivate the inhibitor. There was a correlation between the release of sulfate anions from the inhibitor molecule on incubation with HCl (0.2 N) at 100 degrees C and loss of inhibitory properties of the molecule. It is suggested that the presence of sulfate ester linkages in the inhibitor molecule play an important role in the inhibition process.
Uyeda
M
M
Laboratory of Medicinal Microbiology, Faculty of Pharmaceutical Sciences, Kumamoto University, Japan.
Yoshida
A
A
Oshima
H
H
Suzuki
K
K
Shibata
M
M
D004791:Enzyme Inhibitors; D005964:Glucosyltransferases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification / Q000494:pharmacology; D007700:Kinetics; D008847:Micromonospora; D009930:Organic Chemicals; D011480:Protease Inhibitors / Q000494:pharmacology*; D013295:Streptococcus mutans / Q000201:enzymology*
D004791:Enzyme Inhibitors; D009930:Organic Chemicals; D011480:Protease Inhibitors; C058961:micromonospora glucosyl transferase inhibitor; D005964:Glucosyltransferases