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Results 1 - 10 of 323 > >>
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EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more - 287909, 287920, 287932, 287950
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more activity depends non-linearly on protein concentration in the range 0.00003-0.003 mM. With increasing concentrations the apparently hyperbolic substrate saturation curves turn into sigmoidal ones 287953
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more enzyme kinetics, the recombinant enzyme exhibits about 6fold higher Km value toward 1,3-bisPGA compared to Ga3P. kcat in the way of Ga3P oxidation is about 5fold higher than in the opposite direction, thus resulting in a similar catalytic efficiency (kcat/Km) of the enzyme for the forward and the reverse reactions 762770
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more kinetic analysis and thermodynamics of purified euthermic and torpid enzyme 743402
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more kinetic isotope effects. The enzyme exhibits a kinetic mechanism in which first NAD+, then D-glyceraldehyde 3-phosphate bind to the active site resulting in the formation of a covalently bound thiohemiacetal intermediate. After oxidation of the thiohemiacetal and subsequent nucleotide exchange (NADH off, NAD+ on), the binding of inorganic phosphate and phosphorolysis yields the product 3-phospho-D-glyceroyl phosphate. Solvent and multiple kinetic isotope effects revealed that the first halfreaction is rate limiting and utilizes a step-wise mechanism for thiohemiacetal oxidation via a transient alkoxide to promote hydride transfer and thioester formation. steady-state kinetics 741758
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more kinetics, overview 742014
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more Michaelis-Menten kinetics 743738, 763540
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more the enzyme presents allosteric positive cooperativity for substrates NAD+ and D-glyceraldehyde 3-phosphate, kinetic analysis, overview 743740
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more the mammalian enzyme shows negative cooperativity 743613
Show all pathways known for 1.2.1.12Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.12-999 - more the recombinant protein shows no cooperativity towards glyceraldehyde 3-phosphate as a substrate, Michaelis-Menten kinetics with glyceraldehyde 3-phosphate as a substrate 741965
Results 1 - 10 of 323 > >>
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