Flexibility and reactivity in promiscuous enzymes.
Best of both worlds: The interplay of active site reactivity and the dynamic character of proteins allows enzymes to be promiscuous and--sometimes--remarkably efficient at the same time. This review analyses the roles structural flexibility and chemical reactivity play in the catalytic mechanism of selected enzymes.
Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
Pietro
P
Gatti-Lafranconi
Florian
F
Hollfelder
D055162:Biocatalysis; D020134:Catalytic Domain; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D004950:Esterases / Q000737:chemistry / Q000378:metabolism; D016961:Rhizobium leguminosarum / Q000201:enzymology; D013379:Substrate Specificity
D004798:Enzymes; D004950:Esterases; C101869:phosphonate monoester hydrolase