Asparagine biosynthesis by the Novikoff Hepatoma isolation, purification, property, and mechanism studies of the enzyme system.

An enzyme system that catalyzes the conversion of Laspartate-W to asparagine-W in the presence of glutamine, ATP, and Mg++ has been purified 108-fold from a homogenate of the Novikoff hepatoma. ATP is converted to adenosine 5’-phosphate and inorganic pyrophosphate, and substitution of hydroxylamine for glutamine yields P-aspartylhydroxamate. The data suggest that the synthesis of asparagine in mammalian tissues proceeds through the intermediate fl-aspartyladenylate.