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

  • Biosci Biotechnol Biochem. 2018 Jan;82(1):110-113. doi: 10.1080/09168451.2017.1403887.
Seiya Watanabe  1  2  3 ,  Daichi Morimoto  2  4 ,  Fumiyasu Fukumori  5 ,  Yasuo Watanabe  1  2
Affiliations
  • 1. a Department of Bioscience, Graduate School of Agriculture , Ehime University , Matsuyama , Japan.
  • 2. b Faculty of Agriculture , Ehime University , Matsuyama , Japan.
  • 3. c Center for Marine Environmental Studies , Ehime University , Matsuyama , Japan.
  • 4. e Graduate School of Agriculture , Kyoto University , Kyoto , Japan.
  • 5. d Faculty of Food and Nutritional Sciences , Toyo University , Gunma , Japan.
PMID: 29191113 DOI: 10.1080/09168451.2017.1403887
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.

Keywords
C4DHyp, cis-4-hydroxy-D-proline; INT, p-iodonitrotetrazolium violet; L-hydroxyproline metabolism; NBT, nitroblue tetrazolium; PMS, phenazine methosulfate; Sinorhizobium meliloti; SmhypO, hypO gene from Sinorhizobium meliloti; T4DHyp, trans-4-hydroxy-D-proline; T4LHyp, trans-4-hydroxy-L-proline; cis-4-hydroxy-D-proline dehydrogenase.
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