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http://purl.uniprot.org/citations/27824095http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27824095http://www.w3.org/2000/01/rdf-schema#comment"L-asparaginase (L-ASNase) (EC 3.5.1.1) is an important enzyme for the treatment of acute lymphoblastic leukaemia. Currently, the enzyme is obtained from bacteria, Escherichia coli and Erwinia chrysanthemi. The bacterial enzymes family is subdivided in type I and type II; nevertheless, only type II have been employed in therapeutic proceedings. However, bacterial enzymes are susceptible to induce immune responses, leading to a high incidence of adverse effects compromising the effectiveness of the treatment. Therefore, alternative sources of L-ASNase may be useful to reduce toxicity and enhance efficacy. The yeast Saccharomyces cerevisiae has the ASP1 gene responsible for encoding L-asparaginase 1 (ScASNase1), an enzyme predicted as type II, like bacterial therapeutic isoforms, but it has been poorly studied. Here we characterised ScASNase1 using a recombinant enzyme purified by affinity chromatography. ScASNase1 has specific activity of 196.2 U/mg and allosteric behaviour, like type I enzymes, but with a low K0.5 = 75 μM like therapeutic type II. We showed through site-directed mutagenesis that the T64-Y78-T141-K215 residues are involved in catalysis. Furthermore, ScASNase1 showed cytotoxicity for the MOLT-4 leukemic cell lineage. Our data show that ScASNase1 has characteristics described for the two subfamilies of l-asparaginase, types I and II, and may have promising antineoplastic properties."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.org/dc/terms/identifier"doi:10.1038/srep36239"xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"Monteiro G."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"Schultz L."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"de Oliveira M.A."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"Costa I.M."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"Pessoa A."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"Leite M.S."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"Farsky S.H."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/author"de Araujo Bianchi Pedra B."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/name"Sci Rep"xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/pages"36239"xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/title"Recombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activity."xsd:string
http://purl.uniprot.org/citations/27824095http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/27824095http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27824095
http://purl.uniprot.org/citations/27824095http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27824095
http://purl.uniprot.org/uniprot/P38986#attribution-D03094CFD9DEADA884ABCABE0A796DD1http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/27824095
http://purl.uniprot.org/uniprot/#_A0A6A5Q1U3-mappedCitation-27824095http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27824095
http://purl.uniprot.org/uniprot/#_P38986-mappedCitation-27824095http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27824095
http://purl.uniprot.org/uniprot/A0A6A5Q1U3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27824095
http://purl.uniprot.org/uniprot/P38986http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27824095