دورية أكاديمية
أعرض في EDS

Unravelling biochemical and structural features of Bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies.

التفاصيل البيبلوغرافية
العنوان: Unravelling biochemical and structural features of Bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies.
المؤلفون: Briganti L; Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São Carlense 400 - Centro, São Carlos, SP 13560-970, Brazil., Manzine LR; Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São Carlense 400 - Centro, São Carlos, SP 13560-970, Brazil., de Mello Capetti CC; Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São Carlense 400 - Centro, São Carlos, SP 13560-970, Brazil., de Araújo EA; Brazilian Synchrotron Light Laboratory (LNLS), Brazilian Center for Research in Energy and Materials, Campinas 13083-970, São Paulo, Brazil., de Oliveira Arnoldi Pellegrini V; Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São Carlense 400 - Centro, São Carlos, SP 13560-970, Brazil., Guimaraes FEG; Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São Carlense 400 - Centro, São Carlos, SP 13560-970, Brazil., de Oliveira Neto M; Departamento de Física e Biofísica, Instituto de Biociências de Botucatu, Universidade Estadual Paulista, Distrito de Rubião Jr. s/n, Botucatu 18618-000, SP, Brazil., Polikarpov I; Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São Carlense 400 - Centro, São Carlos, SP 13560-970, Brazil. Electronic address: ipolikarpov@ifsc.usp.br.
المصدر: International journal of biological macromolecules [Int J Biol Macromol] 2024 Aug; Vol. 274 (Pt 2), pp. 133182. Date of Electronic Publication: 2024 Jun 15.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
مواضيع طبية MeSH: Bacillus licheniformis*/enzymology , Bacillus licheniformis*/genetics , Catalytic Domain* , Mutagenesis, Site-Directed*, Crystallography, X-Ray ; Molecular Dynamics Simulation ; Mannosidases/chemistry ; Mannosidases/genetics ; Mannosidases/metabolism ; Substrate Specificity ; Hydrolysis ; Tetroses/chemistry ; Tetroses/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Protein Conformation ; Mannans/chemistry ; Mannans/metabolism ; beta-Mannosidase/chemistry ; beta-Mannosidase/genetics ; beta-Mannosidase/metabolism ; Models, Molecular ; Molecular Docking Simulation ; Oligosaccharides
مستخلص: Glycoside hydrolase family 5 (GH5) encompasses enzymes with several different activities, including endo-1,4-β-mannosidases. These enzymes are involved in mannan degradation, and have a number of biotechnological applications, such as mannooligosaccharide prebiotics production, stain removal and dyes decolorization, to name a few. Despite the importance of GH5 enzymes, only a few members of subfamily 7 were structurally characterized. In the present work, biochemical and structural characterization of Bacillus licheniformis GH5 mannanase, BlMan5_7 were performed and the enzyme cleavage pattern was analyzed, showing that BlMan5_7 requires at least 5 occupied subsites to perform efficient hydrolysis. Additionally, crystallographic structure at 1.3 Å resolution was determined and mannoheptaose (M7) was docked into the active site to investigate the interactions between substrate and enzyme through molecular dynamic (MD) simulations, revealing the existence of a - 4 subsite, which might explain the generation of mannotetraose (M4) as an enzyme product. Biotechnological application of the enzyme in stain removal was investigated, demonstrating that BlMan5_7 addition to washing solution greatly improves mannan-based stain elimination.
Competing Interests: Declaration of competing interest None.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
فهرسة مساهمة: Keywords: Bacillus licheniformis; Crystallographic structure; GH5_7 mannanase
المشرفين على المادة: EC 3.2.1.- (Mannosidases)
3634-02-4 (mannotetraose)
0 (Tetroses)
0 (Bacterial Proteins)
0 (Mannans)
EC 3.2.1.25 (beta-Mannosidase)
0 (Oligosaccharides)
تواريخ الأحداث: Date Created: 20240617 Date Completed: 20240730 Latest Revision: 20240730
رمز التحديث: 20240730
DOI: 10.1016/j.ijbiomac.2024.133182
PMID: 38885857
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0003
DOI:10.1016/j.ijbiomac.2024.133182