2.3.3.16 additional information - additional information mutants, overview 488060 2.3.3.16 0.00037 - S-carboxymethyl-CoA 25°C, pH and temperature not specified in the publication, competitive inhibition versus acetyl-CoA 724900 2.3.3.16 0.00037 - S-carboxymethyl-CoA pH and temperature not specified in the publication, competitively inhibition versus acetyl-CoA 724900 2.3.3.16 0.0017 - NADH mutant enzyme R109L 659254 2.3.3.16 0.0024 - propionyl-CoA versus acetyl-CoA, competitive 488059 2.3.3.16 0.0024 - S-carboxymethyl-CoA 25°C, pH and temperature not specified in the publication, non-competitive inhibition versus oxaloacetate 724900 2.3.3.16 0.0024 - S-carboxymethyl-CoA non-competitively inhibition versus oxaloacetate, pH and temperature not specified in the publication 724900 2.3.3.16 0.0028 - NADH wild-type enzyme 659254 2.3.3.16 0.003 - oxaloacetate mutant enzyme H110A, in presence of 0.1 M KCl 659254 2.3.3.16 0.004 - oxaloacetate mutant enzyme T204A, in presence of 0.1 M KCl 659254 2.3.3.16 0.005 - oxaloacetate mutant enzyme R163L, in presence of 0.1 M KCl 659254 2.3.3.16 0.007 - oxaloacetate mutant enzyme R109L, in presence of 0.1 M KCl 659254 2.3.3.16 0.01 - oxaloacetate mutant enzyme Q182A, in presence of 0.1 M KCl 659254 2.3.3.16 0.012 - NADH in 20 mM Tris-HCl 488028 2.3.3.16 0.017 - oxaloacetate mutant enzyme N189A, in presence of 0.1 M KCl 659254 2.3.3.16 0.018 - NADH mutant enzyme Q182A 659254 2.3.3.16 0.018 - oxaloacetate mutant enzyme T111A, in presence of 0.1 M KCl 659254 2.3.3.16 0.0225 - propionyl-CoA versus oxaloacetate, noncompetitive 488059 2.3.3.16 0.023 - NADH - 488078 2.3.3.16 0.026 - oxaloacetate wild-type enzyme, in presence of 0.1 M KCl 659254 2.3.3.16 0.037 - oxaloacetate mutant enzyme K167A, in presence of 0.1 M KCl 659254 2.3.3.16 0.051 - oxaloacetate mutant enzyme Y145A, in presence of 0.1 M KCl 659254 2.3.3.16 0.08 - NADH mutant enzyme T111A 659254 2.3.3.16 0.1 - NADH below 799 2.3.3.16 0.11 - CoA - 488034 2.3.3.16 0.121 - NADH mutant enzyme H110A 659254 2.3.3.16 0.125 - ATP versus acetyl-CoA 488059 2.3.3.16 0.165 - NADH mutant enzyme T204A 659254 2.3.3.16 0.242 - NADH mutant enzyme N189A 659254 2.3.3.16 0.3 - 2-oxoglutarate below 799 2.3.3.16 0.3 - ATP below 799 2.3.3.16 0.33 - ATP mitochondrial isozyme 488047 2.3.3.16 0.36 - ATP - 488048 2.3.3.16 0.38 - 2-oxoglutarate versus oxaloacetate, competitive 488059 2.3.3.16 0.4 - ATP - 488043 2.3.3.16 0.4 - NADH mutant enzyme R163L 659254 2.3.3.16 0.4 12 NADH strains X and Hanham 488044 2.3.3.16 0.5 - ATP - 488043 2.3.3.16 0.63 - NADH mutant enzyme K167A 659254 2.3.3.16 0.66 - NADH in 0.1 M Tris-HCl 488028 2.3.3.16 0.75 - ATP versus acetyl-CoA 488030 2.3.3.16 0.76 - 2-oxoglutarate wild-type 488060 2.3.3.16 0.79 - NADH mutant enzyme Y145A 659254 2.3.3.16 0.8 - NADPH - 488043 2.3.3.16 0.9 - ATP - 799 2.3.3.16 1 - ATP - 488030 2.3.3.16 1.9 - ATP - 799 2.3.3.16 1.9 - ATP 30°C, pH 8, versus acetyl-CoA 657610 2.3.3.16 2.2 - 2-oxoglutarate - 799 2.3.3.16 2.2 - ATP - 799 2.3.3.16 2.4 - citrate pH not specified in the publication, temperature not specified in the publication 755975 2.3.3.16 2.6 - ATP glyoxysomal isozyme 488047 2.3.3.16 3 4 NADH - 488048 2.3.3.16 3.2 - NADH - 799 2.3.3.16 3.5 - ATP - 488029 2.3.3.16 3.5 - NADH - 488048 2.3.3.16 4.2 - ATP - 799 2.3.3.16 4.34 - ATP substrate oxaloacetate, pH 8.0, 25°C 758181 2.3.3.16 4.4 - NADH - 488043 2.3.3.16 4.41 - NADH substrate oxaloacetate, pH 8.0, 25°C 758181 2.3.3.16 4.6 - NADH - 799 2.3.3.16 4.9 - NADPH - 488043 2.3.3.16 5 - ATP - 488039 2.3.3.16 5.2 - NADH - 799 2.3.3.16 5.4 - 2-oxoglutarate - 799 2.3.3.16 5.4 - NADH - 799 2.3.3.16 5.6 - ATP - 799 2.3.3.16 7.19 - citrate substrate oxaloacetate, pH 8.0, 25°C 758181 2.3.3.16 7.5 - ATP - 488038 2.3.3.16 7.96 - NADH substrate acetyl-CoA, pH 8.0, 25°C 758181 2.3.3.16 8.93 - ATP pH not specified in the publication, temperature not specified in the publication 755975 2.3.3.16 10 - NADH above 799 2.3.3.16 10.4 - NADH - 488043 2.3.3.16 20 - 2-oxoglutarate above 799 2.3.3.16 30 - ATP above 799