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Information on EC - asparagine synthase (glutamine-hydrolysing)

for references in articles please use BRENDA:EC6.3.5.4
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IUBMB Comments
The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel [5,6]. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a beta-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine .
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
l-asparaginase, asnase, asparagine synthetase b, glutamine-dependent asparagine synthetase, pvas2, taasn1, ste10, glutamine-dependent amidotransferase, taasn2, asparagine synthetase1, more
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram