title: Structure and functioning mechanism of transketolase.
abstract: Studies of thiamine diphosphate-dependent enzymes appear to have commenced in 1937, with the isolation of the coenzyme of yeast pyruvate decarboxylase, which was demonstrated to be a diphosphoric ester of thiamine. For quite a long time, these studies were largely focused on enzymes decarboxylating α-keto acids, such as pyruvate decarboxylase and pyruvate dehydrogenase complexes. Transketolase, discovered independently by Racker and Horecker in 1953 (and named by Racker) [1], did not receive much attention until 1992, when crystal X-ray structure analysis of the enzyme from Saccharomyces cerevisiae was performed [2]. These data, together with the results of site-directed mutagenesis, made it possible to understand in detail the mechanism of thiamine diphosphate-dependent catalysis. Some progress was also made in studies of the functional properties of transketolase. The last review on transketolase, which was fairly complete, appeared in 1998 [3]. Therefore, the publication of this paper should not seem premature.
authors.affiliation: A.N.Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russian Federation. Electronic address: kochetov@genebee.msu.ru.
authors.forename: German A
authors.initials: GA
authors.lastname: Kochetov
authors.affiliation: A.N.Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russian Federation.
authors.forename: Olga N
authors.initials: ON
authors.lastname: Solovjeva
mesh_terms: D001665:Binding Sites; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism; D003067:Coenzymes / Q000737:chemistry* / Q000378:metabolism; D006019:Glycolysis / Q000502:physiology; D007700:Kinetics; D008958:Models, Molecular; D010427:Pentose Phosphate Pathway / Q000502:physiology; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D013835:Thiamine Pyrophosphate / Q000737:chemistry* / Q000378:metabolism; D014174:Transketolase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D003067:Coenzymes; D029701:Saccharomyces cerevisiae Proteins; D014174:Transketolase; D013835:Thiamine Pyrophosphate; D002118:Calcium
keywords: Conformational mobility of enzyme molecule; Nonequivalence of active sites; ThDP-dependent catalysis; Thiamine diphosphate; Transketolase; Transketolase-like proteins