Next Article in Journal
Preliminary Results on the Evaluation of the Occurrence of Tetrodotoxin Associated to Marine Vibrio spp. in Bivalves from the Galician Rias (Northwest of Spain)
Previous Article in Journal
Collagens of Poriferan Origin
Previous Article in Special Issue
Dichloroisocoumarins with Potential Anti-Inflammatory Activity from the Mangrove Endophytic Fungus Ascomycota sp. CYSK-4
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessArticle
Mar. Drugs 2018, 16(3), 80; https://doi.org/10.3390/md16030080

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.
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)
View Full-Text   |   Download PDF [2665 KB, uploaded 5 March 2018]   |  

Abstract

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
Figures

Figure 1

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. (CC BY 4.0).

Supplementary material

Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

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

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top