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Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family.

التفاصيل البيبلوغرافية
العنوان: Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family.
المؤلفون: Miguel-Ruano V; Department of Crystallography and Structural Biology, Institute of Physical-Chemistry 'Rocasolano', Spanish National Research Council (CSIC), Madrid, Spain., Rivera I; Department of Crystallography and Structural Biology, Institute of Physical-Chemistry 'Rocasolano', Spanish National Research Council (CSIC), Madrid, Spain., Rajkovic J; Biochemistry Laboratory, CITACA-Agri-Food Research and Transfer Cluster, Campus Auga, University of Vigo, Ourense, Spain., Knapik K; EXPRELA Group, University A Coruña, Science Faculty, Advanced Scientific Research Center (CICA), A Coruña, Spain., Torrado A; Biochemistry Laboratory, CITACA-Agri-Food Research and Transfer Cluster, Campus Auga, University of Vigo, Ourense, Spain., Otero JM; GalChimia, S.A., Cebreiro, A Coruña, Spain., Beneventi E; GalChimia, S.A., Cebreiro, A Coruña, Spain., Becerra M; EXPRELA Group, University A Coruña, Science Faculty, Advanced Scientific Research Center (CICA), A Coruña, Spain., Sánchez-Costa M; Department of Molecular Biology, Center for Molecular Biology 'Severo Ochoa' (UAM-CSIC), Autonomous University of Madrid, Madrid, Spain., Hidalgo A; Department of Molecular Biology, Center for Molecular Biology 'Severo Ochoa' (UAM-CSIC), Autonomous University of Madrid, Madrid, Spain., Berenguer J; Department of Molecular Biology, Center for Molecular Biology 'Severo Ochoa' (UAM-CSIC), Autonomous University of Madrid, Madrid, Spain., González-Siso MI; EXPRELA Group, University A Coruña, Science Faculty, Advanced Scientific Research Center (CICA), A Coruña, Spain., Cruces J; GalChimia, S.A., Cebreiro, A Coruña, Spain., Rúa ML; Biochemistry Laboratory, CITACA-Agri-Food Research and Transfer Cluster, Campus Auga, University of Vigo, Ourense, Spain., Hermoso JA; Department of Crystallography and Structural Biology, Institute of Physical-Chemistry 'Rocasolano', Spanish National Research Council (CSIC), Madrid, Spain.
المصدر: Computational and structural biotechnology journal [Comput Struct Biotechnol J] 2021 Feb 10; Vol. 19, pp. 1214-1232. Date of Electronic Publication: 2021 Feb 10 (Print Publication: 2021).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology Country of Publication: Netherlands NLM ID: 101585369 Publication Model: eCollection Cited Medium: Print ISSN: 2001-0370 (Print) Linking ISSN: 20010370 NLM ISO Abbreviation: Comput Struct Biotechnol J Subsets: PubMed not MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology
Original Publication: Gothenburg, Sweden : Research Network of Computational and Structural Biotechnology
مستخلص: A novel esterase, EstD11, has been discovered in a hot spring metagenomic library. It is a thermophilic and thermostable esterase with an optimum temperature of 60°C. A detailed substrate preference analysis of EstD11 was done using a library of chromogenic ester substrate that revealed the broad substrate specificity of EstD11 with significant measurable activity against 16 substrates with varied chain length, steric hindrance, aromaticity and flexibility of the linker between the carboxyl and the alcohol moiety of the ester. The tridimensional structures of EstD11 and the inactive mutant have been determined at atomic resolutions. Structural and bioinformatic analysis, confirm that EstD11 belongs to the family IV, the hormone-sensitive lipase (HSL) family, from the α/β-hydrolase superfamily. The canonical α/β-hydrolase domain is completed by a cap domain, composed by two subdomains that can unmask of the active site to allow the substrate to enter. Eight crystallographic complexes were solved with different substrates and reaction products that allowed identification of the hot-spots in the active site underlying the specificity of the protein. Crystallization and/or incubation of EstD11 at high temperature provided unique information on cap dynamics and a first glimpse of enzymatic activity in vivo . Very interestingly, we have discovered a unique Met zipper lining the active site and the cap domains that could be essential in pivotal aspects as thermo-stability and substrate promiscuity in EstD11.
Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(© 2021 The Authors.)
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فهرسة مساهمة: Keywords: CHCA, cyclohexane carboxylic acid; CMC, critical micellar concentration; CV, column volume; Crystal structure; DMSO, dimethyl sulfoxide; DSF, Differential scanning fluorimetry; Enzyme-substrate complex; FLU, fluorescein; HSL, hormone-sensitive lipase; LDAO, N,N-dimethyldodecylamine N-oxide; MNP, methyl-naproxen; Metagenomic; NP, naproxen; PPL, Porcine Pancreatic Lipase; Thermophilic esterase; pNP, 4-nitrophenol; α/β hydrolase fold
تواريخ الأحداث: Date Created: 20210308 Latest Revision: 20240407
رمز التحديث: 20240407
مُعرف محوري في PubMed: PMC7905190
DOI: 10.1016/j.csbj.2021.01.047
PMID: 33680362
قاعدة البيانات: MEDLINE
الوصف
تدمد:2001-0370
DOI:10.1016/j.csbj.2021.01.047