ligase

[li´gās, lig´ās]

any of a class of enzymes that catalyze the joining together of two molecules coupled with the breakdown of a pyrophosphate bond in ATP or a similar triphosphate.

DNA ligase either of two enzymes that join two double-helical molecules of DNA together to make a longer DNA molecule.

ligase chain reaction a type of DNA amplification that uses DNA ligase to link chains and amplify the template containing the sequence in question.

li·gase

(lī'gās),

Generic term for enzymes (EC class 6) catalyzing the joining of two molecules coupled with the breakdown of a pyrophosphate bond in ATP or a similar compound.
See also: synthetase.

Farlex Partner Medical Dictionary © Farlex 2012

ligase

(lī′gās′, -gāz′)

Any of a class of enzymes that catalyze the linkage of two large molecules.

li·gase

(lī'gās)

Generic term for enzymes (EC class 6) catalyzing the joining of two molecules coupled with the breakdown of a pyrophosphate bond in adenosine triphosphate or a similar compound.
See also: synthetase

Medical Dictionary for the Health Professions and Nursing © Farlex 2012

ligase

An ENZYME that promotes the linkage of chemical groups. Also known as a synthetase.

Collins Dictionary of Medicine © Robert M. Youngson 2004, 2005

ligase

an enzyme that catalyses the joining of short molecules into longer ones, for example, DNA LIGASE.

Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005

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References in periodicals archive

Shankar et al., "Regulation of mitophagy by the Gp78 E3 ubiquitin ligase," Molecular Biology of the Cell, vol.

Mitochondrial quality control: decommissioning power plants in neurodegenerative diseases

Dai et al., "Human HRD1 Is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum," The Journal of Biological Chemistry, vol.

A novel peptide-based SILAC method to identify the posttranslational modifications provides evidence for unconventional ubiquitination in the ER-associated degradation pathway

An extraordinary example of the variability of UPS function in dendritic morphogenesis is the E3 ligase Mind bomb-1 (Mib1).

Breaking it down: the ubiquitin proteasome system in neuronal morphogenesis

The single subunit transmembrane E3 ligase gene related to anergy in lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins across the cell membrane.

Grail suppresses stress-induced apoptosis and colony formation in oral cancer cells

NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN.

Upregulation of Neural Precursor Cell Expressed Developmentally Downregulated 4-1 is Associated with Poor Prognosis and Chemoresistance in Lung Adenocarcinoma

Zhang et al., "Ubiquitin ligase Smurf1 mediates tumor necrosis factor-induced systemic bone loss by promoting proteasomal degradation of bone morphogenetic signaling proteins," The Journal of Biological Chemistry, vol.

Deubiquitinating Enzymes and Bone Remodeling

TNFAIP3 is a ubiquitin-editing enzyme that participates in ubiquitin ligase and deubiquitinase activities.

Whole Exome Sequencing and Molecular Modeling of a Missense Variant in TNFAIP3 That Segregates with Disease in a Family with Chronic Urticaria and Angioedema

To test whether Hbo1 alone has ubiquitin E3 ligase activity, an array of E2 ubiquitin conjugating enzymes for self-ubiquitination of commercial Hbo1 protein were screened by mixing commercial recombinant Hbo1 protein with E1, E2, ATP, and biotinylated ubiquitin and probing with Cy5-conjugated streptavidin (Fig.

Intrinsic ubiquitin E3 ligase activity of histone acetyltransferase Hbo1 for estrogen receptor [alpha]

The glutamate-cysteine ligase modifier subunit (GCLM) and the glutamate-cysteine ligase catalytic subunit (GCLC) form the glutathione cysteine ligase (GCL) that catalyzes the conversion of glutamate and cysteine into y-glutamyl cysteine, a glutathione precursor [4].

Exercise induced upregulation of glutamate-cysteine ligase catalytic subunit and glutamate-cysteine ligase modifier subunit gene expression in Thoroughbred horses

Located at the N-terminal region of pCAF, lies a domain containing ubiquitin E3 ligase activity [23].

Pulling a Ligase out of a "HAT": pCAF Mediates Ubiquitination of the Class II Transactivator

Tomkinson, "The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase," Nucleic Acids Research, vol.

Overexpression of PCNA Attenuates Oxidative Stress-Caused Delay of Gap-Filling during Repair of UV-Induced DNA Damage

These results suggested that siRNA-mediated knockdown of PIASy inhibited the sumoylation of IKK[gamma] and the activation of NF-[kappa]B inflammatory signaling; in other words, the SUMO E3 ligase PIASy plays an important role in the activation of NF-[kappa]B signaling induced by high glucose.

SUMO E3 Ligase PIASy Mediates High Glucose-Induced Activation of NF-[kappa]B Inflammatory Signaling in Rat Mesangial Cells