Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Dec 24:9:787791.
doi: 10.3389/fbioe.2021.787791. eCollection 2021.

Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy

Affiliations
Review

Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy

Thien-Kim Le et al. Front Bioeng Biotechnol. .

Abstract

One-carbon (C1) chemicals are potential building blocks for cheap and sustainable re-sources such as methane, methanol, formaldehyde, formate, carbon monoxide, and more. These resources have the potential to be made into raw materials for various products used in our daily life or precursors for pharmaceuticals through biological and chemical processes. Among the soluble C1 substrates, methanol is regarded as a biorenewable platform feedstock because nearly all bioresources can be converted into methanol through syngas. Synthetic methylotrophy can be exploited to produce fuels and chemicals using methanol as a feedstock that integrates natural or artificial methanol assimilation pathways in platform microorganisms. In the methanol utilization in methylotrophy, methanol dehydrogenase (Mdh) is a primary enzyme that converts methanol to formaldehyde. The discovery of new Mdhs and engineering of present Mdhs have been attempted to develop synthetic methylotrophic bacteria. In this review, we describe Mdhs, including in terms of their enzyme properties and engineering for desired activity. In addition, we specifically focus on the application of various Mdhs for synthetic methylotrophy.

Keywords: C1 gas; assimilation; formaldehyde; methanol dehydrogenase; synthetic methylotrophy.

PubMed Disclaimer

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Natural methane and methanol utilization pathways in methylotrophs.
FIGURE 2
FIGURE 2
Three classes of methanol dehydrogenases (Mdhs).

References

    1. Anthony C., Williams P. (2003). The Structure and Mechanism of Methanol Dehydrogenase. Biochim. Biophys. Acta 1647 (1-2), 18–23. 10.1016/s1570-9639(03)00042-6 - DOI - PubMed
    1. Anthony C. (1982). The Biochemistry of Methylotrophs. London, England: Academic Press.
    1. Anthony C. (2004). The Quinoprotein Dehydrogenases for Methanol and Glucose. Arch. Biochem. Biophys. 428 (1), 2–9. 10.1016/j.abb.2004.03.038 - DOI - PubMed
    1. Anthony C., Zatman L. J. (1967). Prosthetic Group of Alcohol Dehydrogenase of Pseudomonas Sp. M27-A New Oxidoreductase Prosthetic Group. Biochem. J. 104 (3), 960. 10.1042/bj1040960 - DOI - PMC - PubMed
    1. Anthony C., Zatman L. (1965). The Microbial Oxidation of Methanol. The Alcohol Dehydrogenase of Pseudomonas Sp. M27. Biochem. J. 96, 808–812. 10.1042/bj0960808 - DOI - PMC - PubMed

LinkOut - more resources