A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases.
An in silico survey of the -1 subsite of all known 3D-structures of O-glycoside hydrolases containing a suitably positioned ligand has led to the recognition -- apparently without exceptions -- of a transition state stabilising hydrophobic platform which is complementary to a crucial hydrophobic patch of the ligand. This platform is family-specific and highly conserved. A comprehensive list is given with examples of enzymes belonging to 33 different families. Several typical constellations of platform - protein residues are described.
Nerinckx
W
W
Department of Biochemistry, Physiology and Microbiology, Ghent University, K L Ledeganckstraat 35, B-9000 Gent, Belgium. wim.nerinckx@rug.ac.be
Desmet
T
T
Claeyssens
M
M
D000818:Animals; D001665:Binding Sites; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism*; D013045:Species Specificity
D006026:Glycoside Hydrolases