Transamination in Leptospira biflexa.

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Abstract
The ability of whole cells and dialyzed cell-free extracts of L. biflexa to carry out transamination reactions was examined. Quantitative transamination experiments were done using a-ketoglutarate, pyruvate, or oxalacetate as amino acceptors and a number of amino acids as amino donors. The results, though similar to transamination reactions in other tissues, emphasize the importance of amino acid metabolism in the leptospirae. Dialysis of cell-free extracts against a chelating agent demonstrated that pyridoxal phosphate is the coenzyme of the leptospiral transaminasas.

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