Functional flexibility of the transketolase molecule

Transketolase is the simplest representative of the thiamine di phosphate-d ependent enzymes. It was the first of these enzymes for which X-ray analysi s was performed. Based on the data of X-ray studies and using the mutagenes is technique, the nature of functional groups of the enzyme involved in the interaction with substrates and cofactors and in the coenzyme activation w as defined. Thus, considerable achievements have been made in studying the structure of transketolase. However, there is relatively little information on the conformational flexibility of the enzyme molecule while it is funct ioning, i.e., during its interaction with cofactors and substrates and in t he course of intermediate product formation. This review summarizes mainly the results obtained in the author's group, as well as those rare data on t his subject that Could be found in literature.