Ligases


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Ligases

 

(or synthetases), a class of enzymes that catalyze the joining together of two molecules. They play an important role in the most significant anabolic processes—the biosynthesis of proteins, fats, and carbohydrates. Reactions catalyzed by ligases take place at the expense of energy released during the breakdown of adenosine triphosphate (ATP) or a similar triphosphate. The term “ligase” is also applied to synthesizing enzymes that act without the participation of nucleoside triphosphates.

References in periodicals archive ?
Programmed destruction of target proteins with small molecules that utilize a ubiquitin ligase complex has garnered great interest in recent years.
Although it is still unknown what types of ubiquitin E3 ligases are involved and whether neddylation of DCUN1D2 is involved in these pathological conditions, it is necessary to examine the role of neddylation in pathological conditions of the PNS.
There are over 250 Nrf2-targeted genes, including NAD(P)H:quinone oxidoreductase-1 (NQO1), heme oxygenase-1 (HO-1), glutamate cysteine ligase, glutathione S-transferase, glutathione peroxidase, catalase, superoxide dismutase, and thioredoxin UDP-glucuronosyltransferase [23].
E3 ubiquitin ligase is an enzyme that catalyzes covalent binding of multiple ubiquitin proteins to its substrates and enhances degradation of the substrate proteins in the proteasome.
Her team found that SIAH ubiquitin ligases were specifically and markedly "upregulated" in pancreatic cancers.
Poster 1039: "A High Throughput Screening Platform for the Identification of Small Molecule Inhibitors of the E3 Ligase E6AP" by I.
Ubiquitylation typically targets individual proteins, and high selectivity is achieved by a plethora of ubiquitin-conjugating enzymes and ligases.
Cozzarelli elucidated the nature of DNA architecture and growth through enzymologic studies of polymerases, ligases, recombinases, and topoisomerases.
This amplification detects both structural genes encoding D-alanine--D-alanine ligases and glycopeptide resistance genes.
Solaris Therapeutics (Bucks), working on a unique approach to protein misfolding through ring domains of E3 ligases responsible for ubiquitinization.
Secondly, candidate ligases, carboxylases and the cognate acyltransferase domains that specifically recruit the unusual extender units will be studied in vitro for substrate specificity and for their ability to accept non-natural substrates bearing chemical functionality.
While ligation based adapter addition is a hallmark of most NGS library preparations, it is well known that ligases can introduce sequence dependent bias, an un-desirable side effect.