Characterization of cis -4-hydroxy-D-proline dehydrogenase from Sinorhizobium meliloti.

ThehypOgene fromSinorhizobium meliloti, located within thetrans-4-hydroxy-L-proline metabolic gene cluster, was first successfully expressed in the hostPseudomonas putida. Purified HypO protein functioned as a FAD-containingcis-4-hydroxy-D-proline dehydrogenase with a homomeric structure. In contrast to other known enzymes, significant activity for D-proline was found, confirming a previously proposed potential involvement in D-proline metabolism. [ABSTRACT FROM PUBLISHER]