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Ligand thiamine diphosphate
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Basic Ligand Information
Related pathways
BRENDA
KEGG
MetaCyc
thiamine diphosphate biosynthesis I (E. coli), thiamine diphosphate biosynthesis II (Bacillus), thiamine diphosphate biosynthesis III (Staphylococcus), thiamine diphosphate biosynthesis IV (eukaryotes), thiamine diphosphate salvage I 
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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 (3330 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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348950, 348976, 393995, 348954, 348980, 348969, 348970, 348973, 348978, 348971, 655234, 690088, 687353, 687748, 687812, 713120, 710828, 711033, 712006, 712786, 348948
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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
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
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
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
-
485992, 485995, 486023, 486004, 486009, 485993, 485997, 485994, 485996, 485999, 486001, 485998, 658646, 672285, 691270, 691298, 691423, 685766, 691433, 692925, 693289, 693291, 694066, 691763, 692645, 736993, 735401, 735416, 735415, 735708, 735721, 735856, 735938, 736657, 756629, 756713, 756894, 756895, 757041, 757197, 757326, 757895, 758271, 758383, 758509, 756232, 776492
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
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
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
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
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
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 one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, two glycolaldehyde molecules are bound to both coenzyme rings and the erythrulose molecule is bound to a thiazole ring
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
in the one-substrate transketolase reaction, water is covalently bound to thiamine diphosphate after the formation of holotransketolase, and a carbanion is formed as a result of its elimination
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
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+
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+
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
out-of-plane distortion of a xylulose-5-phosphate - thiamine diphosphate adduct results from an intramolecular hydrogen bond in a favorable geometry. The long length of the scissile C2x?C3x bond is mostly a product of significant electron-withdrawing effects on the carbon atoms making this bond
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
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
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
similar to wild-type, variant S385Y/D469T/R520Q exists as high- and low-affinity forms in presence of Mg2+. The binding cooperativity changes from positive to non-cooperative as [Mg2+] increases and peaks at 4 mM for wild-type
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
-
-
-
-
-
-
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
-
395873, 395911, 395886, 657852, 658223, 677228, 675377, 674354, 671290, 667251, 671854, 672568, 672866, 672865, 672867, 697061, 697349, 699740, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 733241, 733658, 733685, 733747, 733745, 733744, 733987, 756475, 756622, 756700, 755711, 757918, 757919, 758241, 758232, 758259, 756075, 756209
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
in the crystal structure with amidosulfuron, cofactor is modified to a peracetate adduct
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required as cofactor
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
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-
-
-
-
-
failure of DXP producting in the absence of thiamine diphosphate indicates its absolute requirement for the enzymatic reaction
failure of DXP producting in the absence of thiamine diphosphate indicates its absolute requirement for the enzymatic reaction
failure of DXP producting in the absence of thiamine diphosphate indicates its absolute requirement for the enzymatic reaction
failure of DXP producting in the absence of thiamine diphosphate indicates its absolute requirement for the enzymatic reaction
failure of DXP producting in the absence of thiamine diphosphate indicates its absolute requirement for the enzymatic reaction
failure of DXP producting in the absence of thiamine diphosphate indicates its absolute requirement for the enzymatic reaction
formation of C2alpha-lactylthiamin diphosphate intermediate is observed
formation of C2alpha-lactylthiamin diphosphate intermediate is observed
formation of C2alpha-lactylthiamin diphosphate intermediate is observed
formation of C2alpha-lactylthiamin diphosphate intermediate is observed
formation of C2alpha-lactylthiamin diphosphate intermediate is observed
formation of C2alpha-lactylthiamin diphosphate intermediate is observed
sequence contains a thiamin diphosphate-binding domain in the N-terminus, which begins and concludes with the highly conserved sequences -GDG- and - LNDN-, respectively
sequence contains a thiamin diphosphate-binding domain in the N-terminus, which begins and concludes with the highly conserved sequences -GDG- and - LNDN-, respectively
sequence contains a thiamin diphosphate-binding domain in the N-terminus, which begins and concludes with the highly conserved sequences -GDG- and - LNDN-, respectively
sequence contains a thiamin diphosphate-binding domain in the N-terminus, which begins and concludes with the highly conserved sequences -GDG- and - LNDN-, respectively
sequence contains a thiamin diphosphate-binding domain in the N-terminus, which begins and concludes with the highly conserved sequences -GDG- and - LNDN-, respectively
sequence contains a thiamin diphosphate-binding domain in the N-terminus, which begins and concludes with the highly conserved sequences -GDG- and - LNDN-, respectively
the DXS3 class of proteins does not contain a conserved thiamine diphosphate binding site
the DXS3 class of proteins does not contain a conserved thiamine diphosphate binding site
the DXS3 class of proteins does not contain a conserved thiamine diphosphate binding site
the DXS3 class of proteins does not contain a conserved thiamine diphosphate binding site
the DXS3 class of proteins does not contain a conserved thiamine diphosphate binding site
the DXS3 class of proteins does not contain a conserved thiamine diphosphate binding site
thiamine diphosphate is bound to its pocket via H-bonds with Leu254, Arg 255, Lys66, His306, Arg337, Arg73, and Glu95
thiamine diphosphate is bound to its pocket via H-bonds with Leu254, Arg 255, Lys66, His306, Arg337, Arg73, and Glu95
thiamine diphosphate is bound to its pocket via H-bonds with Leu254, Arg 255, Lys66, His306, Arg337, Arg73, and Glu95
thiamine diphosphate is bound to its pocket via H-bonds with Leu254, Arg 255, Lys66, His306, Arg337, Arg73, and Glu95
thiamine diphosphate is bound to its pocket via H-bonds with Leu254, Arg 255, Lys66, His306, Arg337, Arg73, and Glu95
thiamine diphosphate is bound to its pocket via H-bonds with Leu254, Arg 255, Lys66, His306, Arg337, Arg73, and Glu95
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
in absence of any residue that can act as a general acid/base the cofactor N4' atom is a critical component of the mechanism
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
Km value of wild-type 0.008 mM, mutant S391A 0.017 mM, mutant R395K 0.0022 mM, respectively
thiamine diphosphate-dependent enzyme, the thiamine diphosphate binding region is situated across two subunits of the closely associated dimer, two binding regions per dimer, binding is facilitated by a combination of hydrogen bonding and formation of a complex with a single Mg2+ ion, mode of binding, CEAS must rely heavily on the cofactor for general acid/base catalysis
thiamine diphosphate-dependent enzyme, the thiamine diphosphate binding region is situated across two subunits of the closely associated dimer, two binding regions per dimer, binding is facilitated by a combination of hydrogen bonding and formation of a complex with a single Mg2+ ion, mode of binding, CEAS must rely heavily on the cofactor for general acid/base catalysis
dependent on, 0.8 ThDP per enzyme monomer, ThDP binding motif, overview
dependent on, 0.8 ThDP per enzyme monomer, ThDP binding motif, overview
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
-
650079, 649510, 650447, 666806, 665422, 683005, 679923, 679914, 679924, 679569, 678843, 682443, 691427, 686477, 692402, 692733, 693587, 693703, 690432, 694588, 694835, 695198, 690431, 690937, 691428, 691435, 691443, 691441, 702341, 704470, 706270, 714220, 714005, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
bound to the active site located at the interface of the alpha and gamma domains
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
coenzyme, bound in the interface between two subunits, binds pH-dependently
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, active center, at the interface of the alpha and gamma domains
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, cofactor is located between the alpha and the gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, located at the active site at the interface of the alpha and gamma domains
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
the structure of glyoxylate carboligase reveals that there is no glutamate in a position to interact with N1 of thiamine diphosphate, the position homologous to the conserved glutamate is occupied by Val51
the structure of glyoxylate carboligase reveals that there is no glutamate in a position to interact with N1 of thiamine diphosphate, the position homologous to the conserved glutamate is occupied by Val51
the structure of glyoxylate carboligase reveals that there is no glutamate in a position to interact with N1 of thiamine diphosphate, the position homologous to the conserved glutamate is occupied by Val51
the structure of glyoxylate carboligase reveals that there is no glutamate in a position to interact with N1 of thiamine diphosphate, the position homologous to the conserved glutamate is occupied by Val51
the structure of glyoxylate carboligase reveals that there is no glutamate in a position to interact with N1 of thiamine diphosphate, the position homologous to the conserved glutamate is occupied by Val51
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dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
dependent on, structural binding environment, overview. The V-conformation is assisted by the presence of a fulcrum residue, Leu403, located directly below the cofactor, the V-conformation results in a N4'-C2 distance of 3.1 A
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
ThDP, dependent on. Density functional theory calculations identify off-cycle intermediate species of the ThDP cofactor that can have implications on the kinetics of the reaction. ThDP performs nucleophilic/covalent catalysis
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
the enzyme avoids formation of a benzoyl anion by addition of enzyme-bound thiamine diphosphate to the carbonyl group of benzoylformate, producing enzyme-bound 2-(2-mandelyl)thiamine diphosphate
enzyme is a non-oxidative thiamin diphosphate-dependent alpha-oxoacid decarboxylase
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0.1 mM, 8fold increase in activity. 39fold increase in activity in presence of 0.1 mM thiamine diphosphate and 5 mM Mg2+
dependent on, IpdC is preincubated with 15mM thiamine diphosphate/Mg2+ in 10 mM Mes-NaOH at 25°C for 30 min to saturate the enzyme with cofactor
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
dependent on. Residue F120 may contribute to a hydrophobic environment for the stabilization of the ThDP cofactor
primary sequence of Ppd contains signature typical for enzymes requiring thiamine diphosphate
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dependent, only in the presence of both cofactors, 0.015 mM Mg2+ and thiamine diphosphate, a significant enzymatic stabilisation is achieved
dependent, only in the presence of both cofactors, 0.015 mM Mg2+ and thiamine diphosphate, a significant enzymatic stabilisation is achieved
dependent, only in the presence of both cofactors, 0.015 mM Mg2+ and thiamine diphosphate, a significant enzymatic stabilisation is achieved
dependent, the optimal concentration is 0.1-5 mM, a significant loss of activity is observed with a concentration below 0.01 mM
dependent, the optimal concentration is 0.1-5 mM, a significant loss of activity is observed with a concentration below 0.01 mM
dependent, the optimal concentration is 0.1-5 mM, a significant loss of activity is observed with a concentration below 0.01 mM
Activator in Enzyme-catalyzed Reactions (186 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
KGDHC is saturated with endogenous tightly bound thiamine diphosphate, but the addition of exogenous thiamine diphosphate to the reaction medium leads to a marked increase in KGDHC affinity to 2-oxoglutarate
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E1 binds thiamine diphosphate, possessing two thiamine-binding pockets located between alpha and beta subunits
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
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94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
-
94884, 349050, 349051, 349055, 349057, 349058, 349059, 349063, 349075, 349056, 349072, 349073, 349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061, 349047, 349048, 349054, 349082, 349086, 349040, 349049, 349078, 349091, 349069, 349076, 349080, 349081, 349083, 349084, 349089
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
the cofactor is fixed at the two ends in separate domains, suspending a comparatively mobile thiazolium ring between them
the cofactor is fixed at the two ends in separate domains, suspending a comparatively mobile thiazolium ring between them
the cofactor is fixed at the two ends in separate domains, suspending a comparatively mobile thiazolium ring between them
Inhibitor in Enzyme-catalyzed Reactions (40 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
2-oxoisopentanoate protects, not pyruvate; non- or uncompetitively inhibition of K+-stimulated activity
-
inhibits phosphorylation of wild-type E1, mutant E1-S303A and mutant E1-D296A/S303A, but not phosphorylation of mutant E1-H292A
-
soluble enzyme, at levels of substrate 2 to 3 times Km, no inhibition of membrane-associated enzyme
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
Metals and Ions (6 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
3D Structure of Enzyme-Ligand-Complex (PDB) (1451 results)
EC NUMBER
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (32 results)
EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
KM Value (61 results)
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
Ki Value (2 results)
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
IC50 Value (3 results)
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
References & Links
Literature References (782)
Links to other databases for thiamine diphosphate
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Release 2026.1 (March 2026)
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