Structural and functional diversity of asparaginases: Overview and recommendations for a revised nomenclature

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorKing's College London-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.creatorda Silva, Leonardo Schultz [UNESP]-
Autor(es): dc.creatorDoonan, Liam B.-
Autor(es): dc.creatorPessoa, Adalberto-
Autor(es): dc.creatorde Oliveira, Marcos Antonio [UNESP]-
Autor(es): dc.creatorLong, Paul F.-
Data de aceite: dc.date.accessioned2022-02-22T00:46:10Z-
Data de disponibilização: dc.date.available2022-02-22T00:46:10Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2020-12-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/bab.2127-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/206099-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/206099-
Descrição: dc.descriptionAsparaginases (ASNases) are a large and structurally diverse group of enzymes ubiquitous amongst archaea, bacteria and eukaryotes, that catalyze hydrolysis of asparagine to aspartate and ammonia. Bacterial ASNases are important biopharmaceuticals for the treatment of acute lymphoblastic leukemia, although some patients experience adverse allergic side effects during treatment with these protein therapeutics. ASNases are currently divided into three families: plant-type ASNases, Rhizobium etli-type ASNases and bacterial-type ASNases. This system is outdated as both bacterial-type and plant-type families also include archaeal, bacterial and eukaryotic enzymes, each with their own distinct characteristics. Herein, phylogenetic studies allied to tertiary structural analyses are described with the aim of proposing a revised and more robust classification system that considers the biochemical diversity of ASNases. Accordingly, based on distinct peptide domains, phylogenetic data, structural analysis and functional characteristics, we recommend that ASNases now be divided into three new distinct classes containing subgroups according to structural and functional aspects. Using this new classification scheme, 25 ASNases were identified as candidates for future new lead discovery.-
Descrição: dc.descriptionInstituto de Biociências Universidade Estadual Paulista (UNESP)-
Descrição: dc.descriptionInstitute of Pharmaceutical Science School of Cancer & Pharmaceutical Sciences Faculty of Life Sciences & Medicine King's College London-
Descrição: dc.descriptionDepartamento de Tecnologia Tecnologia Bioquímico-Farmacêuticas Faculdade de Ciencias Farmaceuticas Universidade de São Paulo-
Descrição: dc.descriptionInstituto de Biociências Universidade Estadual Paulista (UNESP)-
Idioma: dc.languageen-
Relação: dc.relationBiotechnology and Applied Biochemistry-
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Palavras-chave: dc.subjectbiopharmaceuticals-
Palavras-chave: dc.subjectbioprospecting-
Palavras-chave: dc.subjectclassification-
Palavras-chave: dc.subjectenzyme diversity-
Palavras-chave: dc.subjectl-asparaginase-
Palavras-chave: dc.subjectphylogeny-
Título: dc.titleStructural and functional diversity of asparaginases: Overview and recommendations for a revised nomenclature-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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