Abstract
The amino acid proline is not only synthesized as a compatible solute but also used as a carbon and energy source by the moderately halophilic bacterium Halobacillus halophilus. Growth on proline was not affected by the salinity of the medium. Proline was degraded by proline dehydrogenase (ProDH) and Δ(1) -pyrroline-5-carboxylate dehydrogenase (P5CDH) to glutamate via Δ(1) -pyrroline-5-carboxylate. The basic biochemical parameters for ProDH and P5CDH activities were obtained for both in cell free extracts. The encoding genes were identified. H. halophilus has two isogenes each for prodh and p5cdh. prodh2 and p5cdh2 form an operon (put operon) whose mRNA is highly abundant in proline-grown cells. Expression of the put operon was also upregulated by salinity and late growth phase in glucose-grown cells. Similarly, ProDH and P5CDH activities increased in late exponential growth phase. This observation is in line with the previous notion that the compatible solute proline is degraded in stationary phase (in glucose grown cultures).
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