Characterization of cis-4-hydroxy-D-proline dehydrogenase from Sinorhizobium meliloti. Issue 1 (2nd January 2018)

• Record Type: Journal Article
• Authors: Watanabe, Seiya; Morimoto, Daichi; Fukumori, Fumiyasu; Watanabe, Yasuo
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 82:Issue 1(2018)
• Page Start: 110
• Page End: 113
• Publication Date: 2018-01-02
• Subjects: L-hydroxyproline metabolism -- cis-4-hydroxy-D-proline dehydrogenase -- Sinorhizobium meliloti; T4LHyp, trans-4-hydroxy-L-proline -- C4DHyp, cis-4-hydroxy-D-proline -- T4DHyp, trans-4-hydroxy-D-proline -- INT, p-iodonitrotetrazolium violet -- NBT, nitroblue tetrazolium -- SmhypO, hypO gene from Sinorhizobium meliloti -- PMS, phenazine methosulfate; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2017.1403887
• Languages: English
• ISSNs: 0916-8451

Abstract

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.