Enzymes catalyse virtually all chemical reactions in living organisms, making their rates compatible with life. These proteins, and sometimes RNA’s, have evolved to utilize a range of strategies to achieve incredible rate enhancements in comparison with the corresponding non-catalysed reactions. The study of enzymatic mechanisms is fundamental to elucidate how enzymes work in physical and chemical terms, to guide the rational design of inhibitors, and to help engineer new activities. Here we apply techniques of biochemistry and physical chemistry to unravel the mechanisms of enzymatic reactions involved in bacterial histidine and 5-aminolevulinic acid biosynthesis and in human protein histidine phosphorylation. Particular emphasis is given to transition-state structure and to the role of protein dynamics in energy barrier crossing.
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