Properties of chitin syntheses present in 16S subunits from Mucor rouxii
DOI:
https://doi.org/10.33885/sf.1989.3.738Abstract
Chitin synthetase present in crude wall-membrane fractions from Mucor roux11
was dissociated with digitonin and separated in the form of 16S subun~y centrifugation
in lineal sucrose gradien~s. This enzyme synthesized microfibrils made of
highly crystalline -<-chitin. Chitin synthetase from 16S subunits was extremely unstable
specially once activated by controlled proteolysis. These results plus the
effect of inhibitors of neutral proteases on enzyme stability led to the concl ussion
that 16S subunits contain 3 forms of chitin synthetase in an active equilibrium:
pre·"zymogen", "zymogen" and active enzyme.
General characteristics of 16S-chitin synthetase are very similar to those of
the chitosomal enzyme. However, it was observed that whereas the properties of the
allosteric site of both enzymes were a~most identical, the catalytic site lost affinity
for the substrate, the cofactor Mg +, and the competitive inhibitor, polyoxin D.
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