2.3.1.47 additional information - additional information stopped-flow kinetics of enzyme interaction with L-alanine and D-alanine, steady-state kinetics and thermodynamics 674626 2.3.1.47 additional information - additional information the recombinant KAPA synthase obeys Michaelis-Menten kinetics with respect to pimeloyl-CoA and L-Ala 676580 2.3.1.47 0.001 - pimeloyl-CoA - 487048 2.3.1.47 0.0013 - (S)-8-amino-7-oxononanoic acid calculated from the competitive and uncompetitive constants and the substrate concentration determined in inhibitor experiments, 37°C, pH 8.6 702483 2.3.1.47 0.0014 - S-adenosyl-L-methionine calculated from the competitive and uncompetitive constants and the substrate concentration determined in inhibitor experiments, 37°C, pH 8.6 702483 2.3.1.47 0.0015 - pimeloyl-CoA - 487053 2.3.1.47 0.0015 - pimeloyl-CoA pH 7.7, 25°C, recombinant enzyme 674626 2.3.1.47 0.0016 - pimeloyl-CoA pH 7.5, 30°C, recombinant enzyme 676580 2.3.1.47 0.002 - L-alanine - 487053 2.3.1.47 0.01 - pimeloyl-CoA 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C 718696