Functional Characterization of Four Putative δ¹-Pyrroline-5-Carboxylate Reductases from Bacillus subtilis.

ABSTRACT: In most living organisms, the amino acid proline is synthesized starting from both glutamate and ornithine. In prokaryotes, in the absence of an ornithine cyclodeaminase that has been identified to date only in a small number of soil and plant bacteria, these pathways share the last step, the reduction of δ¹-pyrroline-5-carboxylate (P5C) catalyzed by P5C reductase (EC 1.5.1.2). In several species, multiple forms of P5C reductase have been reported, possibly reflecting the dual function of proline. Aside from its common role as a building block of proteins, proline is indeed also involved in the cellular response to osmotic and oxidative stress conditions. Genome analysis of Bacillus subtilis identifies the presence of four genes (ProH, ProI, ProG, and ComER)

SUBMITTER: Forlani G 

PROVIDER: S-EPMC5539093 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature