Abstract
The metabolism of 14 amino acids by washed cells and cell-free extracts of the Reiter treponeme was investigated. L-Glutamate, L-histidine, L-cysteine, L-arginine, and L-threonine were shown to be deaminated. Carbon dioxide is produced only from L-glutamate and L-histidine. L-Histidine is fermented by washed suspensions of this organism with the rupture of the imidazole ring. Glutamate is metabolized anaerobically with production of ammonia, carbon dioxide, and succinate as the chief end products. Glutamic dehydrogenase was demonstrated spectro-photometrically in sonic extracts. The enzyme system is dependent specifically on diphosphopyridine nucleotide. The enzyme has an opt. pH of approx. 9.7. The reaction is readily reversible; the equilibrium lies far in the direction of L-glutamate formation.