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Updated: Feb 17, 2026

Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
Characterization of cis-4-hydroxy-D-proline dehydrogenase from Sinorhizobium meliloti
Seiya Watanabe1,2,3, Daichi Morimoto2,4, Fumiyasu Fukumori5
1a Department of Bioscience, Graduate School of Agriculture , Ehime University , Matsuyama , Japan.
Abstract:
The hypO gene from Sinorhizobium meliloti, located within the trans-4-hydroxy-L-proline metabolic gene cluster, was first successfully expressed in the host Pseudomonas putida. Purified HypO protein functioned as a FAD-containing cis-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.
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