Crystal structure of a novel xylose isomerase from Streptomyces sp. F-1 revealed the presence of unique features that differ from conventional classes

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Autor(es): dc.contributorBrazilian Ctr Res Energy & Mat CNPEM-
Autor(es): dc.contributorUniversidade Estadual de Campinas (UNICAMP)-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversidade Federal de Mato Grosso do Sul (UFMS)-
Autor(es): dc.creatorMiyamoto, Renan Yuji-
Autor(es): dc.creatorSousa, Amanda Silva de-
Autor(es): dc.creatorVieira, Plinio Salmazo-
Autor(es): dc.creatorMelo, Ricardo Rodrigues de-
Autor(es): dc.creatorScarpassa, Josiane Aniele [UNESP]-
Autor(es): dc.creatorInacio Ramos, Carlos Henrique-
Autor(es): dc.creatorMurakami, Mario Tyago-
Autor(es): dc.creatorRuller, Roberto-
Autor(es): dc.creatorZanphorlin, Leticia Maria-
Data de aceite: dc.date.accessioned2022-02-22T00:05:21Z-
Data de disponibilização: dc.date.available2022-02-22T00:05:21Z-
Data de envio: dc.date.issued2020-12-09-
Data de envio: dc.date.issued2020-12-09-
Data de envio: dc.date.issued2020-05-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.bbagen.2020.129549-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/195264-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/195264-
Descrição: dc.descriptionBackground: Enzymatic isomerization is a promising strategy to solve the problem of xylose fermentation and, consequently, to leverage the production of advanced biofuels and biochemicals. In a previous work, our research group discovered a new strain of Streptomyces with great biotechnological potential due to its ability to produce a broad arsenal of enzymes related to lignocellulose degradation. Methods: We applied a multidisciplinary approach involving enzyme kinetics, biophysical methods, small angle X-ray scattering and X-ray crystallography to investigate two novel xylose isomerases, XylAlF1 and XylA2F1, from this strain. Results: We showed that while XylAlF1 prefers to act at lower temperatures and relatively lower pH, XylA2F1 is extremely stable at higher temperatures and presents a higher turnover number. Structural analysis revealed that XylA1F1 exhibits unique properties in the active site not observed in classical XylAs from classes I and II nor in its ortholog XylA2F1. It encompasses the natural substitutions, M86A and T93K, that create an extra room for substrate accommodation and narrow the active-site entrance, respectively. Such modifications may contribute to the functional differentiation of these enzymes. Conclusions: We have characterized two novel xylose isomerases that display distinct functional behavior and harbor unprecedented amino-acid substitutions in the catalytic interface. General significance: Our findings contribute to a better understanding of the functional and structural aspects of xylose isomerases, which might be instrumental for the valorization of the hemicellulosic fraction of vegetal biomass.-
Descrição: dc.descriptionBrazilian Ctr Res Energy & Mat CNPEM, Brazilian Biorenewables Natl Lab LNBR, Campinas, SP, Brazil-
Descrição: dc.descriptionUniv Estadual Campinas, Inst Biol, Campinas, SP, Brazil-
Descrição: dc.descriptionSao Paulo State Univ, Inst Biosci Letters & Exact Sci, Sao Jose Do Rio Preto, SP, Brazil-
Descrição: dc.descriptionUniv Estadual Campinas, Inst Chem, Campinas, SP, Brazil-
Descrição: dc.descriptionUniv Fed Mato Grosso do Sul, Campo Grande, MS, Brazil-
Descrição: dc.descriptionSao Paulo State Univ, Inst Biosci Letters & Exact Sci, Sao Jose Do Rio Preto, SP, Brazil-
Formato: dc.format10-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier B.V.-
Relação: dc.relationBiochimica Et Biophysica Acta-general Subjects-
???dc.source???: dc.sourceWeb of Science-
Palavras-chave: dc.subjectXylose isomerase-
Palavras-chave: dc.subjectCrystal structure-
Palavras-chave: dc.subjectEnzyme kinetics-
Palavras-chave: dc.subjectStructure-function relationship-
Palavras-chave: dc.subjectHemicellulosic fraction-
Palavras-chave: dc.subjectBiofuels-
Título: dc.titleCrystal structure of a novel xylose isomerase from Streptomyces sp. F-1 revealed the presence of unique features that differ from conventional classes-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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