Characterization of Enzymatic Activity of MlrB and MlrC Proteins Involved in Bacterial Degradation of Cyanotoxins Microcystins

Department of Plant Physiology and Development, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Krakow 30387, Poland

Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Krakow 30387, Poland

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Krakow 30387, Poland

⁴

Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Tykistokatu 6 A, Turku 20520, Finland

Author to whom correspondence should be addressed.

Academic Editor: Luis Botana

Toxins 2016, 8(3), 76; https://doi.org/10.3390/toxins8030076

Received: 12 January 2016 / Revised: 29 February 2016 / Accepted: 7 March 2016 / Published: 16 March 2016

(This article belongs to the Collection Marine and Freshwater Toxins)

View Full-Text Download PDF

Browse Figures

Citation Export

Abstract

Bacterial degradation of toxic microcystins produced by cyanobacteria is a common phenomenon. However, our understanding of the mechanisms of these processes is rudimentary. In this paper several novel discoveries regarding the action of the enzymes of the mlr cluster responsible for microcystin biodegradation are presented using recombinant proteins. In particular, the predicted active sites of the recombinant MlrB and MlrC were analyzed using functional enzymes and their inactive muteins. A new degradation intermediate, a hexapeptide derived from linearized microcystins by MlrC, was discovered. Furthermore, the involvement of MlrA and MlrB in further degradation of the hexapeptides was confirmed and a corrected biochemical pathway of microcystin biodegradation has been proposed. View Full-Text

Keywords: microcystin; biodegradation; recombinant enzymes; biochemical pathway

▼ Show Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary File 1:
Supplementary (PDF, 526 KiB)

Share and Cite

MDPI and ACS Style

Dziga, D.; Zielinska, G.; Wladyka, B.; Bochenska, O.; Maksylewicz, A.; Strzalka, W.; Meriluoto, J. Characterization of Enzymatic Activity of MlrB and MlrC Proteins Involved in Bacterial Degradation of Cyanotoxins Microcystins. Toxins 2016, 8, 76. https://doi.org/10.3390/toxins8030076

AMA Style

Dziga D, Zielinska G, Wladyka B, Bochenska O, Maksylewicz A, Strzalka W, Meriluoto J. Characterization of Enzymatic Activity of MlrB and MlrC Proteins Involved in Bacterial Degradation of Cyanotoxins Microcystins. Toxins. 2016; 8(3):76. https://doi.org/10.3390/toxins8030076

Chicago/Turabian Style

Dziga, Dariusz, Gabriela Zielinska, Benedykt Wladyka, Oliwia Bochenska, Anna Maksylewicz, Wojciech Strzalka, and Jussi Meriluoto. 2016. "Characterization of Enzymatic Activity of MlrB and MlrC Proteins Involved in Bacterial Degradation of Cyanotoxins Microcystins" Toxins 8, no. 3: 76. https://doi.org/10.3390/toxins8030076

Find Other Styles

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Metrics

Abstract views Pdf views Html views

Article Menu

Characterization of Enzymatic Activity of MlrB and MlrC Proteins Involved in Bacterial Degradation of Cyanotoxins Microcystins

Abstract

Supplementary Material

Share and Cite

Article Metrics

Article Access Statistics

Article Access Map by Country/Region

Further Information

Guidelines

MDPI Initiatives

Follow MDPI