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l-Proline dehydrogenases in hyperthermophilic archaea: distribution, function, structure, and application

Applied Microbiology and Biotechnology volume 93, pages 83–93 (2012)Cite this article

Abstract

Dye-linked l-proline dehydrogenase (ProDH) catalyzes the oxidation of l-proline to ∆1-pyrroline-5-carboxylate (P5C) in the presence of artificial electron acceptors. The enzyme is known to be widely distributed in bacteria and eukarya, together with nicotinamide adenine dinucleotide (phosphate)-dependent P5C dehydrogenase, and to function in the metabolism of l-proline to l-glutamate. In addition, over the course of the last decade, three other types of ProDH with molecular compositions completely different from previously known ones have been identified in hyperthermophilic archaea. The first is a heterotetrameric αβγδ-type ProDH, which exhibits both ProDH and reduced nicotinamide adenine dinucleotide dehydrogenase activity and includes two electron transfer proteins. The second is a heterooctameric α4β4-type ProDH, which uses flavin adenine dinucleotide, flavin mononucleotide, adenosine triphosphate, and Fe as cofactors and creates a new electron transfer pathway. The third is a recently identified homodimeric ProDH, which exhibits the greatest thermostability among these archaeal ProDHs. This minireview focuses on the functional and structural properties of these three types of archaeal ProDH and their distribution in archaea. In addition, we will describe the specific application of hyperthermostable ProDH for use in a biosensor and for DNA sensing.

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Acknowledgments

We thank Prof. Hideaki Tsuge for his excellent work to the structural analysis of Ph-ProDH1. We also thank Prof. Shin-ichiro Suye and his students for their crucial contributions to the application of ProDH.

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Affiliations

  1. Analytical Research Center for Experimental Sciences, Saga University, 1, Honjo-machi, Saga, 840-8502, Japan

    Ryushi Kawakami

  2. Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, Fukui, 910-8507, Japan

    Takenori Satomura

  3. Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2392 Ikenobe Miki-cho Kita-gun, Kagawa, 761-0795, Japan

    Haruhiko Sakuraba

  4. Microbial Genetics Division, Institute of Genetic Resources, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, 812-8581, Japan

    Toshihisa Ohshima

Authors
  1. Ryushi Kawakami
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  2. Takenori Satomura
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  3. Haruhiko Sakuraba
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  4. Toshihisa Ohshima
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Correspondence to Toshihisa Ohshima.

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Kawakami, R., Satomura, T., Sakuraba, H. et al. l-Proline dehydrogenases in hyperthermophilic archaea: distribution, function, structure, and application. Appl Microbiol Biotechnol 93, 83–93 (2012). https://doi.org/10.1007/s00253-011-3682-8

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  • DOI: https://doi.org/10.1007/s00253-011-3682-8

Keywords

  • Dye-linked l-proline dehydrogenase
  • Hyperthermophilic archaea
  • Enzyme complex structure
  • Flavoenzyme
  • Catalytic electrode
  • DNA sensing