Al-Hazmi NE, Naguib DM. Plant asparaginase versus microbial asparaginase as anticancer agent. Environ Sci Pollut Res Int. 2022;29(18):27283–93. https://doi.org/10.1007/s11356-021-17925-1.
Article CAS PubMed Google Scholar
Ardalan N, Mirzaie S, Sepahi AA, Khavari-Nejad RA. Novel mutant of Escherichia coli asparaginase II to reduction of the glutaminase activity in treatment of acute lymphocytic leukemia by molecular dynamics simulations and QM-MM studies. Med Hypotheses. 2018;112:7–17. https://doi.org/10.1016/j.mehy.2018.01.004.
Article CAS PubMed Google Scholar
Arnold FH. Directed evolution: bringing new chemistry to life. Angew Chem Int Ed. 2018;57(16):4143–8.
Asselin BL. The three asparaginases. In: Drug resistance in leukemia and lymphoma III. New York: Springer; 1999. p. 621–9.
Avramis VI. Asparaginases: biochemical pharmacology and modes of drug resistance. Anticancer Res. 2012;32(7):2423–37.
Avramis VI, Sencer S, Periclou AP, Sather H, Bostrom BC, Cohen LJ, et al. A randomized comparison of native Escherichia coli asparaginase and polyethylene glycol conjugated asparaginase for treatment of children with newly diagnosed standard-risk acute lymphoblastic leukemia: a Children’s Cancer Group study. Blood. 2002;99(6):1986–94.
SPECTRILA (2020). https://www.bago.com.br/media/files/fcd0f10e5aee4911eb8bee6aabf6ce40ac/faa912de614a611ecaddc6aabf6ce40ac/bula-profissional-de-saude.pdf
Bano M, Sivaramakrishnan VM. Preparation and properties of L-asparaginase from green chillies (Capsicum annum L.). J Biosci. 1980;2(4):291–7. https://doi.org/10.1007/BF02716861.
Bansal S, Gnaneswari D, Mishra P, Kundu B. Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus. Biochem Mosc. 2010;75(3):375–81. https://doi.org/10.1134/S0006297910030144.
Bansal S, Srivastava A, Mukherjee G, Pandey R, Verma AK, Mishra P, Kundu B. Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action. FASEB J. 2012;26(3):1161–71. https://doi.org/10.1096/fj.11-191254.
Article CAS PubMed Google Scholar
Beckett A, Gervais D. What makes a good new therapeutic l-asparaginase? World J Microbiol Biotechnol. 2019;35(10):152. https://doi.org/10.1007/s11274-019-2731-9.
Article CAS PubMed Google Scholar
Belén LH, Lissabet JB, de Oliveira Rangel-Yagui C, Effer B, Monteiro G, Pessoa A, Farías Avendaño JG. A structural in silico analysis of the immunogenicity of l-asparaginase from Escherichia coli and Erwinia carotovora. Biologicals. 2019;59:47–55. https://doi.org/10.1016/j.biologicals.2019.03.003.
Article CAS PubMed Google Scholar
Biçer A, Taslimi P, Yakalı G, Gülçin I, Serdar Gültekin M, Turgut Cin G. Synthesis, characterization, crystal structure of novel bis-thiomethylcyclohexanone derivatives and their inhibitory properties against some metabolic enzymes. Bioorg Chem. 2019;82:393–404. https://doi.org/10.1016/j.bioorg.2018.11.001.
Article CAS PubMed Google Scholar
Boztaş M, Çetinkaya Y, Topal M, Gülçin İ, Menzek A, Şahin E, Tanc M, Supuran CT. Synthesis and carbonic anhydrase isoenzymes I, II, IX, and XII inhibitory effects of dimethoxybromophenol derivatives incorporating cyclopropane moieties. J Med Chem. 2015;58(2):640–50. https://doi.org/10.1021/jm501573b.
Article CAS PubMed Google Scholar
Broome JD. Evidence that the L-asparaginase activity of guinea pig serum is responsible for its antilymphoma effects. Nature. 1961;191(4793):1114–5. https://doi.org/10.1038/1911114a0.
Broome JD. Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects: I. Properties of the L-asparaginase of guinea pig serum in relation to those of the antilymphoma substance. J Exp Med. 1963;118(1):99–120.
CAS PubMed PubMed Central Google Scholar
Brumano LP, da Silva FVS, Costa-Silva TA, Apolinário AC, Santos JHPM, Kleingesinds EK, Monteiro G, Rangel-Yagui CDO, Benyahia B, Junior AP. Development of L-asparaginase biobetters: current research status and review of the desirable quality profiles [review]. Front Bioeng Biotechnol. 2019. https://doi.org/10.3389/fbioe.2018.00212.
Article PubMed PubMed Central Google Scholar
Butreddy A, Kommineni N, Dudhipala N. Exosomes as naturally occurring vehicles for delivery of biopharmaceuticals: insights from drug delivery to clinical perspectives. Nanomaterials (Basel). 2021. https://doi.org/10.3390/nano11061481.
Capuano E, Fogliano V. Acrylamide and 5-hydroxymethylfurfural (HMF): a review on metabolism, toxicity, occurrence in food and mitigation strategies. LWT Food Sci Technol. 2011;44(4):793–810. https://doi.org/10.1016/j.lwt.2010.11.002.
Castro D, Marques A, Almeida M, Paiva G, Bento H, Pedrolli D, Freire M, Tavares A, Santos-Ebinuma V. L-Asparaginase production review: bioprocess design and biochemical characteristics. Appl Microbiol Biotechnol. 2021. https://doi.org/10.1007/s00253-021-11359-y.
Chahardahcherik M, Ashrafi M, Ghasemi Y, Aminlari M. Effect of chemical modification with carboxymethyl dextran on kinetic and structural properties of L-asparaginase. Anal Biochem. 2020;591: 113537. https://doi.org/10.1016/j.ab.2019.113537.
Article CAS PubMed Google Scholar
Chan WK, Lorenzi PL, Anishkin A, Purwaha P, Rogers DM, Sukharev S, et al. The glutaminase activity of L-asparaginase is not required for anticancer activity against ASNS-negative cells. Blood. 2014;123(23):3596–606.
CAS PubMed PubMed Central Google Scholar
Chen R. Enzyme engineering: rational redesign versus directed evolution. Trends Biotechnol. 2001;19(1):13–4. https://doi.org/10.1016/S0167-7799(00)01522-5.
Article CAS PubMed Google Scholar
Clementi A. La désamidation enzymatique de l’asparagine chez les différentes espéces animales et la signification physio logique de sa presence dans l’organisme. Arch Int Physiol. 1922;19(4):369–98.
Cooney DA, Capizzi RL, Handschumacher RE. Evaluation of L-asparagine metabolism in animals and man. Can Res. 1970;30(4):929–35.
Costa-Silva TA, Costa IM, Biasoto HP, Lima GM, Silva C, Pessoa A, Monteiro G. Critical overview of the main features and techniques used for the evaluation of the clinical applicability of L-asparaginase as a biopharmaceutical to treat blood cancer. Blood Rev. 2020;43: 100651. https://doi.org/10.1016/j.blre.2020.100651.
Article CAS PubMed Google Scholar
Costa AR, Rodrigues ME, Henriques M, Oliveira R, Azeredo J. Glycosylation: impact, control and improvement during therapeutic protein production. Crit Rev Biotechnol. 2014;34(4):281–99.
Costa IM, Schultz L, de Araujo Bianchi Pedra B, Leite MSM, Farsky SHP, de Oliveira MA, Pessoa A, Monteiro G. Recombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activity. Sci Rep. 2016;6(1):36239. https://doi.org/10.1038/srep36239.
Article CAS PubMed PubMed Central Google Scholar
da Cunha MC, Silva LC, Sato HH, de Castro RJS. Using response surface methodology to improve the L-asparaginase production by Aspergillus niger under solid-state fermentation. Biocatal Agric Biotechnol. 2018;16:31–6. https://doi.org/10.1016/j.bcab.2018.07.018.
Dantas RC, Caetano LF, Torres ALS, Alves MS, Silva ETMF, Teixeira LPR, Teixeira DC, de Azevedo Moreira R, Fonseca MHG, Gaudêncio Neto S, Martins LT, Furtado GP, Tavares KCS. Expression of a recombinant bacterial l-asparaginase in human cells. BMC Res Notes. 2019;12(1):794. https://doi.org/10.1186/s13104-019-4836-5.
Article CAS PubMed PubMed Central Google Scholar
Darvishi F, Jahanafrooz Z, Mokhtarzadeh A. Microbial L-asparaginase as a promising enzyme for treatment of various cancers. Appl Microbiol Biotechnol. 2022. https://doi.org/10.1007/s00253-022-12086-8.
de Almeida Parizotto L, Krebs Kleingesinds E, Pedrotti M, da Rosa L, Effer B, Meira Lima G, Herkenhoff ME, Li Z, Rinas U, Monteiro G, Pessoa A, Tonso A. Increased glycosylated l-asparaginase production through selection of Pichia pastoris platform and oxygen-methanol control in fed-batches. Biochem Eng J. 2021;173: 108083. https://doi.org/10.1016/j.bej.2021.108083.
De Brabander P, Uitterhaegen E, Delmulle T, De Winter K, Soetaert W. Challenges and progress towards industrial recombinant protein production in yeasts: a review. Biotechnol Adv. 2023;64: 108121. https://doi.org/10.1016/j.biotechadv.2023.108121.
Article CAS PubMed Google Scholar
De Pourcq K, De Schutter K, Callewaert N. Engineering of glycosylation in yeast and other fungi: current state and perspectives. Appl Microbiol Biotechnol. 2010;87(5):1617–31. https://doi.org/10.1007/s00253-010-2721-1.
Article CAS PubMed Google Scholar
Demain AL, Vaishnav P. Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv. 2009;27(3):297–306.
Derst C, Henseling J, Röhm KH. Engineering the substrate specificity of Escherichia coli asparaginase. II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Sci. 2000;9(10):2009–17. https://doi.org/10.1110/ps.9.10.2009.
Comments (0)