ArticleInternational journal of molecular sciences2022
The Emergence of New Catalytic Abilities in an Endoxylanase from Family GH10 by Removing an Intrinsically Disordered Region.
Carlos Gil-Durán, Romina V Sepúlveda, Maximiliano Rojas, Víctor Castro-Fernández, Victoria Guixé, Inmaculada Vaca, Gloria Levicán, Fernando D González-Nilo, María-Cristina Ravanal, Renato Chávez
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In one paragraphArticle in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 · Who and what moneyAuthors and funding
10 authors.
Carlos Gil-DuránFacultad de Química y Biología, Universidad de Santiago de Chile (USACH), Santiago 9170022, Chile.ORCID 0000-0001-9638-6902 Romina V SepúlvedaCenter for Bioinformatics and Integrative Biology, Facultad de Ciencias Biológicas, Universidad Andrés Bello, Santiago 8370146, Chile.ORCID 0000-0001-8899-1440 Maximiliano RojasCenter for Bioinformatics and Integrative Biology, Facultad de Ciencias Biológicas, Universidad Andrés Bello, Santiago 8370146, Chile.
Víctor Castro-FernándezDepartamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago 7800003, Chile.ORCID 0000-0002-4309-6415 Victoria GuixéDepartamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago 7800003, Chile.
Inmaculada VacaDepartamento de Química, Facultad de Ciencias, Universidad de Chile, Santiago 7800003, Chile.
Gloria LevicánFacultad de Química y Biología, Universidad de Santiago de Chile (USACH), Santiago 9170022, Chile.
Fernando D González-NiloCenter for Bioinformatics and Integrative Biology, Facultad de Ciencias Biológicas, Universidad Andrés Bello, Santiago 8370146, Chile.
María-Cristina RavanalInstituto de Ciencia y Tecnología de los Alimentos, Facultad de Ciencias Agrarias y Alimentarias, Universidad Austral de Chile (UACH), Valdivia 5090000, Chile.
Renato ChávezFacultad de Química y Biología, Universidad de Santiago de Chile (USACH), Santiago 9170022, Chile.ORCID 0000-0003-1754-3610 Funding
DICYT-USACH POSTDOC_DICYT Código
021943CHR_POSTDOCFONDEQUIP EQM 140151Instituto Antártico Chileno RG_03-14
6 · The paper itselfAbstract
Endoxylanases belonging to family 10 of the glycoside hydrolases (GH10) are versatile in the use of different substrates. Thus, an understanding of the molecular mechanisms underlying substrate specificities could be very useful in the engineering of GH10 endoxylanases for biotechnological purposes. Herein, we analyzed XynA, an endoxylanase that contains a (β/α)
Indexed as
Amino Acid SequenceCatalysisCatalytic DomainEndo-1,4-beta XylanasesGlycoside HydrolasesHydrolysisSubstrate SpecificityXylansXyloseEndo-1,4-beta XylanasesGlycoside HydrolasesXylansXyloseGH10 endoxylanaseintrinsically disordered regionnew activitiesprotein dynamics(β/α)8-barrel domain
Identifiers
PMID35216436
PMCPMC8874783
What OpenQuestion holds
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