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Open AccessArticle

Molecular Characterization of a Novel N-Acetylneuraminate Lyase from a Deep-Sea Symbiotic Mycoplasma

1
Department of Life Sciences, Institute of Deep-sea Science and Engineering, Chinese Academy of Sciences, Sanya 572000, China
2
College of Earth Sciences, University of Chinese Academy of Sciences, Beijing 100864, China
3
Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100864, China
4
National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China
*
Author to whom correspondence should be addressed.
Mar. Drugs 2018, 16(3), 80; https://doi.org/10.3390/md16030080
Received: 31 January 2018 / Revised: 19 February 2018 / Accepted: 26 February 2018 / Published: 5 March 2018
(This article belongs to the Special Issue Marine Natural Products from Symbiotic Ecosystems)
N-acetylneuraminic acid (Neu5Ac) based novel pharmaceutical agents and diagnostic reagents are highly required in medical fields. However, N-acetylneuraminate lyase(NAL)for Neu5Ac synthesis is not applicable for industry due to its low catalytic efficiency. In this study, we biochemically characterized a deep-sea NAL enzyme (abbreviated form: MyNal) from a symbiotic Mycoplasma inhabiting the stomach of a deep-sea isopod, Bathynomus jamesi. Enzyme kinetic studies of MyNal showed that it exhibited a very low Km for both cleavage and synthesis activities compared to previously described NALs. Though it favors the cleavage process, MyNal out-competes the known NALs with respect to the efficiency of Neu5Ac synthesis and exhibits the highest kcat/Km values. High expression levels of recombinant MyNal could be achieved (9.56 mol L−1 culture) with a stable activity in a wide pH (5.0–9.0) and temperature (40–60 °C) range. All these features indicated that the deep-sea NAL has potential in the industrial production of Neu5Ac. Furthermore, we found that the amino acid 189 of MyNal (equivalent to Phe190 in Escherichia coli NAL), located in the sugar-binding domain, GX189DE, was also involved in conferring its enzymatic features. Therefore, the results of this study improved our understanding of the NALs from different environments and provided a model for protein engineering of NAL for biosynthesis of Neu5Ac. View Full-Text
Keywords: N-acetylneuraminate lyase; Symbiotic microbe; N-acetylneuraminic acid; mycoplasma N-acetylneuraminate lyase; Symbiotic microbe; N-acetylneuraminic acid; mycoplasma
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Wang, S.-L.; Li, Y.-L.; Han, Z.; Chen, X.; Chen, Q.-J.; Wang, Y.; He, L.-S. Molecular Characterization of a Novel N-Acetylneuraminate Lyase from a Deep-Sea Symbiotic Mycoplasma. Mar. Drugs 2018, 16, 80.

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