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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 ...
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. The biosynthesis of aspartate and asparagine from oxaloacetate. Two asparagine synthetases are found in bacteria.
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 .
Applications of asparaginase in cancer therapy take advantage of the fact that acute lymphoblastic leukemia cells and some other suspected tumor cells are unable to synthesize the non-essential amino acid asparagine, whereas normal cells are able to make their own asparagine; thus leukemic cells require a high amount of asparagine. [44]
In enzymology, a glutamin-(asparagin-)ase (EC 3.5.1.38) is an enzyme that catalyzes the chemical reaction. L-glutamine + H 2 O L-glutamate + NH 3. Thus, the two substrates of this enzyme are L-glutamine and H 2 O, whereas its two products are L-glutamate and NH 3.
This article needs attention from an expert in biochemistry.The specific problem is: someone with a solid grasp of the full scope of this subject and of its secondary and advanced teaching literatures needs to address A, the clear structural issues of the article (e.g., general absence of catabolic biosynthetic pathways, insertion of macromolecule anabolic paths before all building blocks ...