The kinetic properties of LDH, such as the Michaelis-Menten constant (Km) and maximum velocity (Vmax), vary among its isoforms. These parameters are influenced by factors such as pH, temperature, and the presence of allosteric effectors. Generally, the Km for pyruvate and NADH is low, indicating a high affinity for these substrates. The Vmax reflects the enzyme's catalytic efficiency and is higher in isoforms that are predominant in tissues with high glycolytic rates.
