ligase


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li·gase

 (lī′gās′, -gāz′)
n.
Any of a class of enzymes that catalyze the linkage of two large molecules.

[Latin ligāre, to bind; see leig- in Indo-European roots + -ase.]

ligase

(ˈlaɪˌɡeɪz)
n
(Biochemistry) any of a class of enzymes that catalyse the formation of covalent bonds and are important in the synthesis and repair of biological molecules, such as DNA

li•gase

(ˈlaɪ geɪs, -geɪz)

n.
an enzyme that catalyzes the joining of two molecules by forming a covalent bond accompanied by the hydrolysis of ATP. Also called synthetase.
[1961; < Latin lig(āre) to tie, bind]
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References in periodicals archive ?
A recent proteomic study has identified a wide array of inter actors for the cytosolic E3 ligase PARKIN; along with cytosolic and nuclear molecular partners, surprisingly, there are also proteins of the mitochondrial matrix [64].
Unlike rhodanine, 2,4-thiazolidinedione derivatives also have remarkable biological activities like antidiabetic [13], antibacterial [14], antifungal [15], antiproliferative effect on vascular smooth muscle [16], aldose reductase inhibitors [17], 15-hydroxyprostaglandin dehydrogenase inhibitors [18] instead of these biological activities 5-benzylidenethiazolidine-2,4-dione derivatives act as inhibitors of MurD ligase [19].
Both lysine and nonlysine ubiquitination of TCRa are dependent upon a functional Hrd1 E3 ligase indicating that this E3 ligase can facilitate both lysine and nonlysine ubiquitination.
Mutation of a vital component of the HIW E3 ligase complex (DFsn) results in elevated levels of Wallenda and phenocopies the hiw mutant, suggesting that ubiquitination of Wallenda by Highwire may control elements of axon morphogenesis [56].
Nurix's technology platform is focused on the manipulation of the ubiquitin system and its component E3 ligases, the key enzymes responsible for controlling protein levels in human cells.
E3 ubiquitin ligase GRAIL controls primary T cell activation and oral tolerance.
T4 DNA Ligase (5u/ul), 5X Rapid ligation Buffer and nuclease-free water were also added in ligation reaction.
Protein ubiquitination by E3 ubiquitin ligase fine-rhythms the defense-associated processes (25,26).
In enterococci, under normal conditions, peptidoglycan synthesis is carried out by a ligase enzyme that joins two molecules of D-alanine to form D-Ala-D-Ala.
If a DNA ligase is present--preferably, one from a thermostable organism so it could have been added during reaction setup, prior to thermal denaturation--it can now act at this nick, converting a previously linear padlock probe into a covalently closed circular molecule; see Figure lc.
Background: The E3 ubiquitin ligase neural precursor cell expressed developmentally downregulated 4-1 (NEDD4-1) negatively regulates phosphatase and tensin homolog deleted on chromosome 10 (PTEN) protein levels through polyubiquitination and proteolysis, but its significance in lung cancer is still unclear.
The E3 enzyme, also known as ubiquitin ligase, acts as a scaffold protein which interacts with the ubiquitin-conjugating enzyme and transfers ubiquitin to protein [18].