Novel cofactors via post-translational modifications of enzyme active sites.
Recent crystallographic and biochemical studies have revealed the existence of numerous novel post-translational modifications within enzyme active sites. These modifications create structural and functional diversity. Although the function and biosynthesis of some of these modifications are well understood, others need further investigation.
Okeley
N M
NM
Department of Chemistry, University of Illinois at Urbana-Champaign, 61801, USA.
van der Donk
W A
WA
D000818:Animals; D001665:Binding Sites; D020134:Catalytic Domain / Q000502:physiology*; D003067:Coenzymes / Q000378:metabolism*; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008667:Metalloproteins; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D014443:Tyrosine / Q000737:chemistry
D003067:Coenzymes; D004798:Enzymes; D008667:Metalloproteins; D014443:Tyrosine