Applied Microbiology and Biotechnology

, Volume 102, Issue 22, pp 9531–9540 | Cite as

Pyrroloquinoline quinone-dependent dehydrogenases of acetic acid bacteria

  • Minenosuke Matsutani
  • Toshiharu YakushiEmail author


Pyrroloquinoline quinone (PQQ)-dependent dehydrogenases (quinoproteins) of acetic acid bacteria (AAB), such as the membrane-bound alcohol dehydrogenase (ADH) and the membrane-bound glucose dehydrogenase, contain PQQ as the prosthetic group. Most of them are located on the periplasmic surface of the cytoplasmic membrane, and function as primary dehydrogenases in cognate substance-oxidizing respiratory chains. Here, we have provided an overview on the function and molecular architecture of AAB quinoproteins, which can be categorized into six groups according to the primary amino acid sequences. Based on the genomic data, we discuss the types of quinoproteins found in AAB genome and how they are distributed. Our analyses indicate that a significant number of uncharacterized orphan quinoproteins are present in AAB. By reviewing recent experimental developments, we discuss how to characterize the as-yet-unknown enzymes. Moreover, our bioinformatics studies also provide insights on how quinoproteins have developed into intricate enzymes. ADH comprises at least two subunits: the quinoprotein dehydrogenase subunit encoded by adhA and the cytochrome subunit encoded by adhB, and the genes are located in a polycistronic transcriptional unit. Findings on stand-alone derivatives of adhA encourage us to speculate on a possible route for ADH development in the evolutional history of AAB. A combination of bioinformatics studies on big genome sequencing data and wet studies assisted with genetic engineering would unravel biochemical functions and physiological role of uncharacterized quinoproteins in AAB, or even in unculturable metagenome.


Acetic acid bacteria Quinoproteins Pyrroloquinoline quinone Genome sequencing 



We are grateful to Kazunobu Matsushita for critically reading the manuscript. We thank Enago ( for the English language review.

Funding information

This work was partially supported by the Japan Society for the Promotion of Science KAKENHI Grant (26830126 to MM; 17K07722 to TY).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflicts of interest.

Ethical statement

In this article, none of the studies that were performed by any of the authors contained human participants or animals.


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© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Division of Agricultural Science, Graduate School of Science and Technology for InnovationYamaguchi UniversityYamaguchiJapan
  2. 2.Department of Biological Chemistry, Faculty of AgricultureYamaguchi UniversityYamaguchiJapan
  3. 3.Research Center for Thermotolerant Microbial ResourcesYamaguchi UniversityYamaguchiJapan

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