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Ligand thiamine diphosphate
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Basic Ligand Information
BRENDA
KEGG
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Show all BRENDA pathways known for thiamine diphosphate
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
In Vivo Product in Enzyme-catalyzed Reactions (9 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
thiamine triphosphate + H2O = thiamine diphosphate + phosphate
ATP + H2O + thiamine diphosphate-[thiamine-binding protein ThiB][side 1] = ADP + phosphate + thiamine diphosphate[side 2] + [thiamine-binding protein ThiB][side 1]
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ATP + H2O + thiamine diphosphate-[thiamine-binding protein][side 1] = ADP + phosphate + thiamine diphosphate[side 2] + [thiamine-binding protein][side 1]
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Substrate in Enzyme-catalyzed Reactions (15 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + thiamine diphosphate = ADP + thiamine triphosphate
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thiamine diphosphate + H2O = thiamine monophosphate + phosphate
Product in Enzyme-catalyzed Reactions (13 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
thiamine triphosphate + H2O = thiamine diphosphate + phosphate
ATP + H2O + thiamine diphosphate-[thiamine-binding protein ThiB][side 1] = ADP + phosphate + thiamine diphosphate[side 2] + [thiamine-binding protein ThiB][side 1]
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ATP + H2O + thiamine diphosphate-[thiamine-binding protein][side 1] = ADP + phosphate + thiamine diphosphate[side 2] + [thiamine-binding protein][side 1]
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Enzyme Cofactor/Cosubstrate (2648 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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348948, 758852, 348977, 348976, 711033, 687353, 687748, 690088, 712786, 655234, 710828, 712006, 713120, 687812, 348954, 348980, 348950, 348971, 348969, 348970, 348973, 348978
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only one of the two thiamine molecules bound to the two active sites of the alpha2beta2 E1 component is in a chemically activated state exhibiting an apparent C2 ionization rate constant of approximately 50 per s at pH 7.6 and 30°C, whereas the thiamine in the inactive site ionizes with a rate that is at least 3 orders of magnitude smaller
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2-oxoglotarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is dependent on thiamine diphosphate. Thiamine diphosphate attacks the alpha-carbon of 2-oxoglutarate and decarboxylates the substrate. The thiamine diphosphate reaction adduct then reductively acylates the lipoyl moiety of EC 2.3.1.61
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activates the 2-oxoglutarate dehydrogenase complex activity, involved in conformational changes
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formation of a precatalytic complex SE between the substrate and the 2-oxoglutarate dehydrogenase component before the catalytic complex ES, in which the substrate is added to the thiamin diphosphate cofactor
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thiamine deficiency results in decreased enzyme complex activity and selective neuronal loss
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thiamine diphosphate is tightly but not covalently bound to the 2-oxoglutarate dehydrogenase component
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PyOd binds one thiamine diphosphate per subunit in the presence of Mg2+, optimum concentration 1 mM
PyOd binds one thiamine diphosphate per subunit in the presence of Mg2+, optimum concentration 1 mM
PyOd binds one thiamine diphosphate per subunit in the presence of Mg2+, optimum concentration 1 mM
PyOd binds one thiamine diphosphate per subunit in the presence of Mg2+, optimum concentration 1 mM
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dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
dependent on, binding structure and determinants, V conformation, K392 is important
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
kcat/Km value for wild-type 20 per mM and s, for mutant H271A 950 per mM and s
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thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to component E1, heterotetrameric cofactor binding fold, cofactor binding prevents phosphorylation of E1b and inactivates it by inducing a disorder-to-order transition of the conserved phosphorylation loop carrying 2 phosphorylation sites Ser292alpha andSer302alpha, cross-talk between thiamine diphosphate and the phosphorylation loop conformation as a feed-forward switch for th complex reaction
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, binding kinetics, wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
bound to E1b component, dissociation constants of recombinant wild-type and mutant E1b components
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
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485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
-
485997, 485992, 485995, 486023, 685766, 691423, 691433, 693289, 693291, 756629, 486004, 486009, 691270, 692645, 757895, 485993, 485994, 485996, 485998, 485999, 658646, 672285, 756232, 486001, 756895, 736993, 694066, 735856, 691763, 757326, 736657, 756713, 756894, 757041, 758383, 691298, 692925, 735708, 735721, 735401, 735415, 735416, 735938, 757197, 758271, 758509
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
additional thiamine does not enhance activity
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form