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

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dc.contributor.authorda Silva, Leonardo Schultz [UNESP]
dc.contributor.authorDoonan, Liam B.
dc.contributor.authorPessoa, Adalberto
dc.contributor.authorde Oliveira, Marcos Antonio [UNESP]
dc.contributor.authorLong, Paul F.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionKing's College London
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2021-06-25T10:26:34Z
dc.date.available2021-06-25T10:26:34Z
dc.date.issued2021-01-01
dc.description.abstractAsparaginases (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 This system is outdated as both bacterial-type and plant-type families also include archaeal, bacterial and eukaryotic enzymes, each with their own distinct characteristics.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.en
dc.description.affiliationInstituto de Biociências Universidade Estadual Paulista (UNESP)
dc.description.affiliationInstitute of Pharmaceutical Science School of Cancer & Pharmaceutical Sciences Faculty of Life Sciences & Medicine King's College London
dc.description.affiliationDepartamento de Tecnologia Tecnologia Bioquímico-Farmacêuticas Faculdade de Ciencias Farmaceuticas Universidade de São Paulo
dc.description.affiliationUnespInstituto de Biociências Universidade Estadual Paulista (UNESP)
dc.identifierhttp://dx.doi.org/10.1002/bab.2127
dc.identifier.citationBiotechnology and Applied Biochemistry.
dc.identifier.doi10.1002/bab.2127
dc.identifier.issn1470-8744
dc.identifier.issn0885-4513
dc.identifier.scopus2-s2.0-85103085102
dc.identifier.urihttp://hdl.handle.net/11449/206099
dc.language.isoeng
dc.relation.ispartofBiotechnology and Applied Biochemistry
dc.sourceScopus
dc.subjectbiopharmaceuticals
dc.subjectbioprospecting
dc.subjectclassification
dc.subjectenzyme diversity
dc.subjectl-asparaginase
dc.subjectphylogeny
dc.titleStructural and functional diversity of asparaginases: Overview and recommendations for a revised nomenclatureen
dc.typeArtigo
unesp.author.orcid0000-0001-6698-4602[5]

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