The biosynthesis of crustacean chitin by a microsomal enzyme from larval brine shrimp.

A microsomal preparation from larval stages of the brine shrimp Artemia salina was found to catalyze the transfer of N-acetyl-D-glucosamine from UDP-N-acetylglucosamine to an endogenous acceptor. The product was identified as chitin by its resistance to extraction with alkali and high concentrations of urea and the liberation of chito-oligosaccharides by treatment with purified chitinases. The enzyme requires Mg2+ for activity and is inhibited by UDP and diflubenzuron, but not by Polyoxin D. The pH optimum is 7.0. The enzyme is not significantly activated by N-acetyl-D-glucosamine nor by trypsin treatment. Incorporation of radioactivity into endogenous acceptor is inhibited by chitodextrins which appear to serve as alternate acceptors. The crustacean enzyme can also utilize exogenous, macromolecular chitin as acceptor. The enzyme, which was partially purified by sucrose step-gradient ultracentrifugation, appears maximally active after 72 h of larval growth.