Molecular Characterization of a Novel N-Acetylneuraminate Lyase from a Deep-Sea Symbiotic Mycoplasma
Wang, Shao-lu1,2; Li, Yun-liang3; Han, Zhuang1; Chen, Xi4; Chen, Qi-jia4; Wang, Yong1; He, Li-sheng1; He, Li-sheng(Chinese Acad Sci, Inst Deep Sea Sci & Engn, Dept Life Sci, Sanya 572000, Peoples R China)
2018-03-01
Source PublicationMARINE DRUGS
Volume16Issue:3
Contribution Rank第1完成单位 ; 第2完成单位 ; 第3完成单位 ; 第4完成单位
AbstractN-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 k(cat)/K(m)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 degrees 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.
SubtypeArticle
KeywordN-acetylneuraminate Lyase Symbiotic Microbe N-acetylneuraminic Acid Mycoplasma
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.3390/md16030080
URL查看原文
Indexed BySCI
Language英语
WOS KeywordSIALIC-ACID METABOLISM ; D-NEURAMINIC ACID ; ESCHERICHIA-COLI ; CLOSTRIDIUM-PERFRINGENS ; HAEMOPHILUS-INFLUENZAE ; ENZYMATIC-SYNTHESIS ; EXPRESSION ; GENE ; PURIFICATION ; DIVERSITY
WOS SubjectChemistry, Medicinal
WOS IDWOS:000428510200006
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Cited Times:3[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.idsse.ac.cn/handle/183446/5966
Collection深海科学研究部_深海生物学研究室_深海无脊椎动物蛋白质组学及分子生物学研究组
Corresponding AuthorHe, Li-sheng; He, Li-sheng(Chinese Acad Sci, Inst Deep Sea Sci & Engn, Dept Life Sci, Sanya 572000, Peoples R China)
Affiliation1.Chinese Acad Sci, Inst Deep Sea Sci & Engn, Dept Life Sci, Sanya 572000, Peoples R China
2.Univ Chinese Acad Sci, Coll Earth Sci, Beijing 100864, Peoples R China
3.Chinese Acad Sci, Inst Phys, Lab Soft Matter Phys, Beijing 100864, Peoples R China
4.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin 300308, Peoples R China
Recommended Citation
GB/T 7714
Wang, Shao-lu,Li, Yun-liang,Han, Zhuang,et al. Molecular Characterization of a Novel N-Acetylneuraminate Lyase from a Deep-Sea Symbiotic Mycoplasma[J]. MARINE DRUGS,2018,16(3).
APA Wang, Shao-lu.,Li, Yun-liang.,Han, Zhuang.,Chen, Xi.,Chen, Qi-jia.,...&He, Li-sheng.(2018).Molecular Characterization of a Novel N-Acetylneuraminate Lyase from a Deep-Sea Symbiotic Mycoplasma.MARINE DRUGS,16(3).
MLA Wang, Shao-lu,et al."Molecular Characterization of a Novel N-Acetylneuraminate Lyase from a Deep-Sea Symbiotic Mycoplasma".MARINE DRUGS 16.3(2018).
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