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Properties of chitin synthase in homogenates from Chironomus cells
Author(s) -
Ludwig Monika,
SpindlerBarth Margarethe,
Spindler KlausDieter
Publication year - 1991
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940180407
Subject(s) - chitin , chitin synthase , uridine triphosphate , chitinase , uridine , biochemistry , uridine diphosphate , substrate (aquarium) , biology , protease , trypsin , allosteric regulation , enzyme , rna , nucleotide , chitosan , ecology , gene
Homogenates of Chironomus cells synthesize chitin as effectively as intact cells. Chitin is produced in a dose‐dependent manner, when GlcN, GlcNAc, or UDP‐GlcNAc is used as precursor. Due to the lability of UDP‐GlcNAc incorporation of this substrate is underestimated. No allosteric effect is observed when GlcN or GlcNAc is used as a substrate. Chitin synthesis is stimulated by Mg 2+ and inhibited by uridine monophosphate (UMP), uridine diphosphate (UDP), and uridine triphosphate (UTP). The apparent temperature optimum is 30°C, the apparent pH optimum is 5.5–6. Addition of the chitinase inhibitor allosamidin does not enhance chitin synthesis significantly. The time course of chitin formation reveals a lag period of about 12 h, which can be overcome by trypsin treatment. Addition of protease inhibitors prevents chitin synthesis.