1887

Abstract

SUMMARY: The solubilized chitin synthetase preparation from the stipes of is activated by its substrate, UDP--acetylglucosamine, and by carbohydrates, in particular -acetylglucosamine, diacetylchitobiose and glucose. Analysis of the results of variation in enzyme activity with UDP-GlcNAc concentration by several methods suggested that this substrate is an allosteric activator, with Hill coefficients close to 2 and 4 at concentrations above and below 0·1 m respectively, and an [S] value of 0·9 m. -acetylglucosamine lessened but did not abolish the sigmoidal shape of the velocity-substrate concentration plot. The chitin synthetase was inhibited by adenine and uridine nucleotides, and uridine diphosphate was a powerful competitive inhibitor. The enzyme preparation also contained a nucleoside diphosphatase activity and the implications of the removal of the inhibitory UDP formed by the chitin synthetase are considered.

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/content/journal/micro/10.1099/00221287-89-1-146
1975-07-01
2021-10-23
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