EC Number |
Cofactor |
Reference |
---|
2.2.1.1 | more |
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 |