New insights into ubiquitin E3 ligase mechanism.
E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.
Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, USA.
Christopher E
CE
Berndsen
1] Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. [2] Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Cynthia
0000000185782969
C
Wolberger
D002384:Catalysis; D008239:Lysine / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D015398:Signal Transduction; D013379:Substrate Specificity; D044763:Ubiquitin-Conjugating Enzymes / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000502:physiology*; D054875:Ubiquitination / Q000502:physiology*; D014452:Ubiquitins / Q000378:metabolism
D014452:Ubiquitins; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases; D008239:Lysine