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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).
The development of JZP-458 as a therapeutic agent for acute lymphoblastic leukemia has achieved significant milestones throughout the years. In 1963, asparaginase (ASNase) was identified as an effective antileukemic agent, and subsequent efforts were made to isolate it from bacterial sources and scale up production for clinical trials. [15]
6-Diazo-5-oxo-L-norleucine (DON) is a glutamine antagonist, which was isolated originally from Streptomyces in a sample of Peruvian soil.This diazo compound is biosynthesized from lysine by three enzymes in bacteria. [2]
The following is a list of antibiotics. The highest division between antibiotics is bactericidal and bacteriostatic. Bactericidals kill bacteria directly, whereas bacteriostatics prevent them from dividing. However, these classifications are based on laboratory behavior.
The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases. [ 7 ] Human proteins containing this domain
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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.