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Nucleotide binding as an allosteric regulatory mechanism for Akkermansia muciniphila ß-N-acetylhexosaminidase Am2136.
Li, Chang-Cheng; Yi, Huan; Wang, Yan-Mei; Tang, Xin-Yue; Zhu, Yi-Bo; Song, Ying-Jie; Zhao, Ning-Lin; Huang, Qin; Mou, Xing-Yu; Luo, Gui-Hua; Liu, Tong-Gen; Yang, Gang-Long; Zeng, Yu-Jiao; Wang, Li-Jie; Tang, Hong; Fan, Gang; Bao, Rui.
Afiliación
  • Li CC; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Yi H; State Key Laboratory of Southwestern Chinese Medicine Resources, College of Ethnic Medicine, Chengdu University of Traditional Chinese Medicine, Chengdu, China.
  • Wang YM; Institute of traditional Chinese medicine, Sichuan College of traditional Chinese Medicine (Sichuan Second Hospital of TCM), Chengdu, China.
  • Tang XY; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Zhu YB; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Song YJ; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Zhao NL; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Huang Q; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Mou XY; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Luo GH; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Liu TG; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Yang GL; School of Biotechnology, Jiangnan University, Chengdu, China.
  • Zeng YJ; State Key Laboratory of Southwestern Chinese Medicine Resources, College of Ethnic Medicine, Chengdu University of Traditional Chinese Medicine, Chengdu, China.
  • Wang LJ; State Key Laboratory of Southwestern Chinese Medicine Resources, College of Ethnic Medicine, Chengdu University of Traditional Chinese Medicine, Chengdu, China.
  • Tang H; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
  • Fan G; State Key Laboratory of Southwestern Chinese Medicine Resources, College of Ethnic Medicine, Chengdu University of Traditional Chinese Medicine, Chengdu, China.
  • Bao R; Division of Infectious Diseases, State Key Laboratory of Biotherapy and Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, China.
Gut Microbes ; 14(1): 2143221, 2022.
Article en En | MEDLINE | ID: mdl-36394293
ß-N-acetylhexosaminidases (EC3.2.1.52), which belong to the glycosyl hydrolase family GH20, are important enzymes for oligosaccharides modification. Numerous microbial ß-N-acetylhexosaminidases have been investigated for applications in biology, biomedicine and biotechnology. Akkermansia muciniphila is an anaerobic intestinal commensal bacterium which possesses specific ß-N-acetylhexosaminidases for gut mucosal layer colonization and mucin degradation. In this study, we assessed the in vitro mucin glycan cleavage activity of the A. muciniphila ß-N-acetylhexosaminidase Am2136 and demonstrated its ability that hydrolyzing the ß-linkages joining N-acetylglucosamine to a wide variety of aglycone residues, which indicated that Am2136 may be a generalist ß-N-acetylhexosaminidase. Structural and enzyme activity assay experiments allowed us to probe the essential function of the inter-domain interactions in ß23-ß33. Importantly, we revealed that the hydrolysis activity of Am2136 was enhanced by nucleotides. We further speculated that this activation mechanism might be associated with the conformational motions between domain III and IV. To our knowledge, this is the first report of nucleotide effector regulated ß-N-acetylhexosaminidase, to reveal its novel biological functions. These findings contribute to understanding the distinct properties within the GH20 family and lay a certain foundation to develop controllable glycan hydrolyzing catalysts.Abbreviations: OD600 - optical cell densities at 600 nm; LB - Luria-Bertani; IPTG - isopropyl ß-D-1-thiogalactopyranoside; PMSF - phenylmethanesulfonyl fluoride; rmsd - root mean square deviation; GlcNAc - N-acetyl-ß-D-glucosamine; GalNAc - N-acetyl-ß-D-galactosamine; Gal - galactose.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Beta-N-Acetilhexosaminidasas / Microbioma Gastrointestinal Idioma: En Revista: Gut Microbes Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Beta-N-Acetilhexosaminidasas / Microbioma Gastrointestinal Idioma: En Revista: Gut Microbes Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos