asparagine synthase (glutamine-hydrolyzing) activity

Definition

Target type: molecularfunction

Catalysis of the reaction: ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate. [EC:6.3.5.4, RHEA:12228]

Asparagine synthase (glutamine-hydrolyzing) activity catalyzes the biosynthesis of asparagine from aspartate and glutamine. This reaction involves the transfer of the amide group from glutamine to aspartate, resulting in the formation of asparagine and glutamate. The enzyme utilizes ATP as an energy source and requires divalent cations like magnesium or manganese for optimal activity. The reaction proceeds in two steps: 1) Glutamine is hydrolyzed to glutamate and ammonia. 2) The ammonia molecule is transferred to aspartate, yielding asparagine. Asparagine synthase plays a crucial role in amino acid metabolism, providing the essential amino acid asparagine for protein synthesis and other cellular processes. It is also involved in nitrogen assimilation, converting ammonia into a less toxic form. The enzyme is found in a wide range of organisms, including bacteria, plants, and animals, highlighting its essential role in life.'
"

Proteins (1)

Compounds (1)