Characterization of cis-4-hydroxy-D-proline dehydrogenase from Sinorhizobium meliloti-Reference-Cited by-同舟云学术

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

Published:2018-01-02 Issue:1 Volume:82 Page:110-113
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Watanabe Seiya¹²³,Morimoto Daichi²⁴,Fukumori Fumiyasu⁵,Watanabe Yasuo¹²

Affiliation:

1. Department of Bioscience, Graduate School of Agriculture, Ehime University, Matsuyama, Japan

2. Faculty of Agriculture, Ehime University, Matsuyama, Japan

3. Center for Marine Environmental Studies, Ehime University, Matsuyama, Japan

4. Graduate School of Agriculture, Kyoto University, Kyoto, Japan

5. Faculty of Food and Nutritional Sciences, Toyo University, Gunma, Japan

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.

Funder

Japan Society for the Promotion of Science

Sumitomo Foundation

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/82/1/110/36844434/bbb0110.pdf

Reference15 articles.

1. Metabolism of proline and the hydroxyprolines;Adams;Annu Rev Biochem,1980

2. α-Ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, D-galactarate and hydroxy-L-proline: molecular and metabolic convergent evolution;Watanabe;J Biol Chem,2007