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Ligases

Definition: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
CAS Number: EC 6.

Ligases Categories.
Carbon-Carbon Ligases - Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.
Carbon-Nitrogen Ligases - Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.
Carbon-Oxygen Ligases - Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.
Carbon-Sulfur Ligases - Enzymes that catalyze the joining of two molecules by the formation of a carbon-sulfur bond. EC 6.2.
Polynucleotide Ligases - Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.
Ubiquitin-Protein Ligase Complexes - Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).

Ligases Definitions and Terms

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