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Information on EC 6.3.2.19 - ubiquitin-protein ligase

for references in articles please use BRENDA:EC6.3.2.19

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Please check here for current data: EC 6.2.1.45
deleted. The ubiquitinylation process is now known to be performed by several enzymes in sequence, starting with EC 6.2.1.45 (ubiquitin-activating enzyme E1) and followed by several transfer reactions, including those of EC 2.3.2.23 (E2 ubiquitin-conjugating enzyme) and EC 2.3.2.27 (RING-type E3 ubiquitin transferase)
IUBMB Comments

Ubiquitin is coupled to protein by a peptide bond between the C-terminal glycine of ubiquitin and ε-amino groups of lysine residues in the protein. An intermediate in the reaction contains one ubiquitin residue bound as a thioester to the enzyme, and a residue of ubiquitin adenylate non-covalently bound to the enzyme.

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