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Results 1 - 10 of 108 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - Chorismic acid Competetive inhibition by I – IV Structur: increase the Km 672622
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol) 674312
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more due to instability of chorismate at higher temperature, a Km value is not determined 692260
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more Michaelis-Menten kinetics 747259, 749355
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more Michaelis-Menten steady-state kinetics 747032
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine 651660
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview 748178
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics 748178
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site 748178
Show all pathways known for 5.4.99.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.5-999 - more The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown 672268
Results 1 - 10 of 108 > >>