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Lactate dehydrogenase ec 1.1.1.27 in phycomyces blakesleeanus


, : Lactate dehydrogenase ec 1.1.1.27 in phycomyces blakesleeanus. Biochemical Journal 203(2): 383-392

An NAD-specific L-(+)-lactate dehydrogenase (EC 1.1.1.27) from the mycelium of P. blakesleeanus N.R.R.L. 1555 (-) was purified .apprx. 700-fold. The enzyme has a MW of 135,000-140,000. The purified enzyme gave a single, catalytically active, protein band after polyacrylamide-gel electrophoresis. It shows optimum activity between pH 6.7-7.5. The P. blakesleeanus lactate dehydrogenase exhibits homotropic interactions with its substrate, pyruvate, and its coenzyme, NADH, at pH 7.5, indicating the existence of multiple binding sites in the enzyme for these ligands. At pH 6.0, the enzyme shows high substrate inhibition by pyruvate. 3-Hydroxypyruvate and 2-oxovalerate exhibit an analogous effect; glyoxylate does not, when tested as substrates at the same pH. At pH 7.5, ATP, which inhibits the enzyme, acts competitively with NADH and pyruvate; at pH 6.0 and low concentrations of ATP, it behaves in an allosteric manner as inhibitor with respect to NADH. GTP has no effect under the same experimental conditions. Partially purified enzyme from sporangiophores behaves in an entirely similar kinetic manner as the one exhibited by the enzyme from mycelium.

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