Research may help better understand the biochemistry underlying catalysis in cells

Investigators from the Institute of Scientific and Industrial Research at Osaka University, together with the Hiroshima Institute of Technology, have announced the discovery of a new protein that allows an organism to conduct an initial and essential step in converting amino acid residues on a crosslinked polypeptide into an enzyme cofactor.

This research may lead to a better understanding of the biochemistry underlying catalysis in cells.

Every living cell is constantly pulsing with an array of biochemical reactions. The rates of these reactions are controlled by special proteins called enzymes, which catalyze specific processes that would otherwise take much longer.

A number of enzymes require specialized molecules called "cofactors," which can help shuttle electrons back and forth during oxidation-reduction reactions. But these cofactors themselves must be produced by the organisms, and often require the assistance of previously existing proteins.

Now, a team of scientists at Osaka University has identified a novel protein called QhpG that is essential for the biogenesis of the enzyme cofactor cysteine tryptophylquinone (CTQ).

By analyzing the mass of the reaction products and determining its crystal structure, they were able to deduce the catalytic function of QhpG, which is adding two hydroxyl groups to a specific tryptophan residue within an active-site subunit QhpC of quinoheme protein amine dehydrogenase, the bacterial enzyme catalyzing the oxidation of various primary amines.

The resulting dihydroxylated tryptophan and an adjacent cysteine residue are finally converted to cofactor CTQ.

However, the action of QhpG is somewhat unusual compared with other protein-modifying enzymes in that it reacts with the tryptophan residue on the QhC triply crosslinked by another enzyme QhpD in a process call post-translation modification. Tryptophan, which naturally contains rings with conjugated bonds, needs the fewest changes to become a quinone cofactor.

"Although several enzymes are known to contain a quinone cofactor derived from a tryptophan residue, the mechanism involved in post-translational modification, as well as the structures of the enzymes involved in their biogenesis, remains poorly understood," lead author Toshinori Oozeki says.

The proteins were obtained by introducing plasmids with the corresponding genes into E. coli bacteria and made into crystals. X-ray diffraction data of the crystal can determine the QhpG protein structure.

The team then used computer software to simulate the docking of the target molecules, the triply crosslinked polypeptide QhpC, based on the crystal structure they found for QhpG. The two post-translational modifications of QhpC are successively carried out in the modification enzyme complex QhpD-QhpG.

Our findings can be applied to development of novel bioactive peptides using enzymes that modify amino acids. Some of these applications include creating new enzymes for the bioremediation of toxic chemicals."

Toshihide Okajima, Study Senior Author, Osaka University

Source:
Journal reference:

Oozeki, T., et al. (2021) Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor. Nature Communications. doi.org/10.1038/s41467-021-21200-9.

Citations

Please use one of the following formats to cite this article in your essay, paper or report:

  • APA

    Osaka University. (2022, December 14). Research may help better understand the biochemistry underlying catalysis in cells. AZoLifeSciences. Retrieved on October 14, 2024 from https://www.azolifesciences.com/news/20210211/Research-may-help-better-understand-the-biochemistry-underlying-catalysis-in-cells.aspx.

  • MLA

    Osaka University. "Research may help better understand the biochemistry underlying catalysis in cells". AZoLifeSciences. 14 October 2024. <https://www.azolifesciences.com/news/20210211/Research-may-help-better-understand-the-biochemistry-underlying-catalysis-in-cells.aspx>.

  • Chicago

    Osaka University. "Research may help better understand the biochemistry underlying catalysis in cells". AZoLifeSciences. https://www.azolifesciences.com/news/20210211/Research-may-help-better-understand-the-biochemistry-underlying-catalysis-in-cells.aspx. (accessed October 14, 2024).

  • Harvard

    Osaka University. 2022. Research may help better understand the biochemistry underlying catalysis in cells. AZoLifeSciences, viewed 14 October 2024, https://www.azolifesciences.com/news/20210211/Research-may-help-better-understand-the-biochemistry-underlying-catalysis-in-cells.aspx.

Comments

The opinions expressed here are the views of the writer and do not necessarily reflect the views and opinions of AZoLifeSciences.
Post a new comment
Post

While we only use edited and approved content for Azthena answers, it may on occasions provide incorrect responses. Please confirm any data provided with the related suppliers or authors. We do not provide medical advice, if you search for medical information you must always consult a medical professional before acting on any information provided.

Your questions, but not your email details will be shared with OpenAI and retained for 30 days in accordance with their privacy principles.

Please do not ask questions that use sensitive or confidential information.

Read the full Terms & Conditions.

You might also like...
Regenerating bone marrow after chemotherapy