2.2.1.1	additional information	as opposed to the kinetically stabilized carbanion/enamine intermediate in transketolase when reconstituted with the native cofactor, 2-(1,2-dihydroxyethyl)-4'-monomethylaminothiamin diphosphate is rapidly released from the active centers during turnover and accumulates in the medium on a preparative scale	690708	
2.2.1.1	NAD+	-	756083	
2.2.1.1	thiamine diphosphate	-	485992, 485993, 485994, 485995, 485996, 485997, 485998, 485999, 486001, 486004, 486009, 486023, 658646, 672285, 685766, 691270, 691298, 691423, 691433, 691763, 692645, 692925, 693289, 693291, 694066, 735401, 735415, 735416, 735708, 735721, 735856, 735938, 736657, 736993, 756232, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509	
2.2.1.1	thiamine diphosphate	0.9 mol thiamine diphosphate per mol subunit	486011	
2.2.1.1	thiamine diphosphate	1 catalytic site per enzyme molecule	486000	
2.2.1.1	thiamine diphosphate	2 catalytic sites per enzyme molecule	486000	
2.2.1.1	thiamine diphosphate	2 mol thiamine diphosphate per mol enzyme	486002, 486003, 486007	
2.2.1.1	thiamine diphosphate	additional thiamine does not enhance activity	486006, 486008, 486011, 486012, 486013	
2.2.1.1	thiamine diphosphate	an active site cleft is formed between the two monomeric units allowing the cofactors thiamine diphosphate and Mg2+ to bind, such that the N-terminal domain I of chain A binds the diphosphate moiety of thiamine diphosphate, and domain II of chain B interacts with the aminopyrimidine ring. The diphosphate moiety of thiamine diphosphate is anchored in place through a number of hydrogen bonds formed with residues Thr48, His85, Ser176, Asp177, Gly178, Asn207, Ile209 and His283 from one monomer, crystallization data	720609	
2.2.1.1	thiamine diphosphate	application of a theoretical model of interactions between ligand-binding sites in a dimeric protein for the analysis of thiamine diphosphate binding to yeast transketolase	672632