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Asparagine synthetase (or aspartate-ammonia ligase) is a chiefly cytoplasmic enzyme that generates asparagine from aspartate. [1] This amidation reaction is similar to that promoted by glutamine synthetase. The enzyme is ubiquitous in its distribution in mammalian organs, but basal expression is relatively low in tissues other than the exocrine ...
Asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4, asparagine synthetase (glutamine-hydrolysing), glutamine-dependent asparagine synthetase, asparagine synthetase B, AS, AS-B) is an enzyme with systematic name L-aspartate:L-glutamine amido-ligase (AMP-forming).
Asparagine (symbol Asn or N [2]) is an α-amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated −NH + 3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic ...
The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming β-aspartyl-AMP. Glutamine donates an ammonium group, which reacts with β-aspartyl-AMP to form asparagine and free AMP.
In enzymology, an aspartate—ammonia ligase (EC 6.3.1.1) is an enzyme that catalyzes the chemical reaction. ATP + L-aspartate + NH 3 AMP + diphosphate + L-asparagine. The 3 substrates of this enzyme are ATP, L-aspartate, and NH 3, whereas its 3 products are AMP, diphosphate, and L-asparagine.
The systematic name of this enzyme class is L-asparagine:tRNAAsn ligase (AMP-forming). Other names in common use include asparaginyl-tRNA synthetase , asparaginyl-transfer ribonucleate synthetase , asparaginyl transfer RNA synthetase , asparaginyl transfer ribonucleic acid synthetase , asparagyl-transfer RNA synthetase , and asparagine translase .
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It hydrolyzes substrates at the C-terminus of asparagine residues. Discovered in 1996 in beans, its homologues have been identified in plants, protozoa, vertebrates, and helminths. The enzyme has been implicated in several human diseases such as cancer, atherosclerosis and inflammation. [4]