Functional flexibility of the transketolase molecule.
Transketolase is the simplest representative of the thiamine diphosphate-dependent enzymes. It was the first of these enzymes for which X-ray analysis was performed. Based on the data of X-ray studies and using the mutagenesis technique, the nature of functional groups of the enzyme involved in the interaction with substrates and cofactors and in the coenzyme activation was 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 functioning, i.e., during its interaction with cofactors and substrates and in the course of intermediate product formation. This review summarizes mainly the results obtained in the author's group, as well as those rare data on this subject that could be found in literature.
Kochetov
G A
GA
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. kochetov@genebee.msu.su
D001665:Binding Sites; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D020035:Holoenzymes / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D018583:Pliability; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013835:Thiamine Pyrophosphate / Q000378:metabolism; D014174:Transketolase / Q000737:chemistry* / Q000378:metabolism*
D020035:Holoenzymes; D014174:Transketolase; D013835:Thiamine Pyrophosphate