| 4359923 |
Bennett NG, Gutfreund H: The kinetics of the interconversion of intermediates of the reaction of pig muscle lactate dehydrogenase with oxidized nicotinamide-adenine dinucleotide and lactate. Biochem J. 1973 Sep;135(1):81-5.
Oxamate competes with pyruvate for the substrate binding site on the E (NADH) complex of pig skeletal muscle lactate dehydrogenase. When this enzyme was mixed with saturating concentrations of NAD (+) and lactate in a stopped-flow rapid-reaction spectrophotometer there was no transient accumulation of enzyme complexes with the reduced nucleotide. The steady-state rate of formation of free NADH was reached within the dead-time of the instrument (3ms). When oxamate was added to inhibit the steady state and to uncouple the equilibration: [Formula: see text] through the rapid formation of E (NADH) (Oxamate), the rate of formation of E (NADH) could be measured by observation of the first turnover. This pH-dependent transient is controlled by the rate of dissociation of pyruvate and the fraction of the enzyme in the form E (NADH) (Pyruvate). |
82(1,1,1,2) |