A novel l-asparaginase from Aquabacterium sp. A7-Y with self-cleavage activation

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• 作者：Zhibin Sun ; Ding Li ; Pingping Liu ; Wenhui Wang ; Kai Ji…
• 关键词：l ; Asparaginase ; Aquabacterium sp. A7 ; Y ; Ntn family of hydrolases ; Self ; cleavage activation
• 刊名：Antonie van Leeuwenhoek
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：109
• 期：1
• 页码：121-130
• 全文大小：914 KB
• 参考文献：Amena S, Vishalakshi N, Prabhakar M, Dayanand A, Lingappa K (2010) Production, purification and characterization of L-asparaginase from Streptomyces gulbargensis. Braz J Microbiol 41:173–178PubMed PubMedCentral CrossRef
  Bansal S, Gnaneswari P, Mishra P, Kundu B (2010) Structural stability and functional analysis of L-asparaginase from Pvrococcus furiosus. Biochemistry (Moscow) 75:375–381CrossRef
  Bejger M, Imiolczyk B, Clavel D, Gilski M, Pajak A, Marsolais F, Jaskolski M (2014) Na+/K+ exchange switches the catalytic apparatus of potassium-dependent plant L-asparaginase. Acta Crystallogr D D70:1854–1872CrossRef
  Borek D, Jaskólski M (2000) Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome. Acta Crystallogr D 56:1505–1507PubMed CrossRef
  Borek D, Jaskólski M (2001) Sequence analysis of enzymes with asparaginase activity. Acta Biochim Pol 48:893–902PubMed
  Borek D, Michalska K, Brzezinski K, Kisiel A, Podkowinski J, Bonthron DT, Krowarsch D, Otlewski J, Jaskolski M (2004) Expression, purification and catalytic activity of Lupinus luteus asparagine β-amidohydrolase and its Escherichia coli homolog. Eur J Biochem 271:3215–3226PubMed CrossRef
  Borkotaky B, Bezbaruah RL (2002) Production and properties of asparaginase from a new Erwinia sp. Folia Microbiol 47:473–476CrossRef
  Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254PubMed CrossRef
  Brannigan JA, Dodson G, Duggleby HJ, Moody PC, Smith JL, Tomchick DR, Murzin AG (1995) A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378:416–419PubMed CrossRef
  Broome JD (1963a) 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 118:99–120PubMed PubMedCentral CrossRef
  Broome JD (1963b) Evidence that the l -asparaginase of guinea pig serum is responsible for its antilymphoma effects. II. Lymphoma 6C3HED cells cultured in a medium devoid of l -asparagine lose their susceptibility to the effects of guinea pig serum in vivo. J Exp Med 118:121–148PubMed PubMedCentral CrossRef
  Bush LA, Herr JC, Wolkowicz M, Sherman NE, Shore A, Flickinger CJ (2002) A novel asparaginase-like protein is a sperm autoantigen in rats. Mol Reprod Dev 62:233–247PubMed CrossRef
  Campbell HA, Mashburn LT, Boyse EA, Old LJ (1967) Two l -asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity. Biochemistry 6:721–730PubMed CrossRef
  Cantor JR, Stone EM, Chantranupong L, Georgiou G (2009) The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity. Biochemistry 48:11026–11031PubMed PubMedCentral CrossRef
  Chohan SM, Rashid N (2013) TK1656, a thermostable l -asparaginase from Thermococcus kodakaraensis, exhibiting highest ever reported enzyme activity. J Biosci Bieng 116:438–443CrossRef
  Eisele N, Linke D, Bitzer K, Na’amnieh S, Nimtz M, Berger RG (2011) The first characterized asparaginase from a basidiomycete, Flammulina velutipes. Bioresour Technol 102:3316–3321PubMed CrossRef
  Evtimova V, Zeillinger R, Kaul S, Weidle UH (2004) Identification of CRASH, a gene deregulated in gynecological tumors. Int J Oncol 24:33–41PubMed
  Guo HC, Xu Q, Buckley D, Guan C (1998) Crystal structures of Flavobacterium glycosylasparaginase: an N-terminal nucleophile hydrolase activated by intramolecular proteolysis. J Biol Chem 273:20205–20212PubMed CrossRef
  Jia M, Xu M, He B, Rao Z (2013) Cloning, expression, and characterization of l -asparaginase from a newly isolated Bacillus subtilis B11-06. J Agric Food Chem 61:9428–9434PubMed CrossRef
  Killander D, Dohlwitz A, Engstedt L, Franzén S, Gahrton G, Gullbring B, Holm G, Holmgren A, Höglund S, Killander A, Lockner D, Mellstedt H, Moe PJ, Palmblad J, Reizenstein P, Skårberg KO, Swedberg B, Udén AM, Wadman B, Wide L, Ahström L (1976) Hypersensitive reaction and antibody formation during l -asparaginase treatment of children and adults with acute leukemia. Cancer 37(1):220–228PubMed CrossRef
  Krishnapura PR, Belur PD, Subramanya S (2015) A critical review on properties and applications of microbial l -asparaginases. Crit Rev Microbiol 13:1–18CrossRef
  Kumar S, Dasu VV, Pakshirajan K (2010) Localization and production of novel l -asparaginase from Pectobacterium carotovorum MTCC 1428. Process Biochem 45:223–229CrossRef
  Kumar S, Dasu VV, Pakshirajan K (2011) Purification and characterization of glutaminase-free l -asparaginase from Pectobacterium carotovorum MTCC 1428. Bioresour Technol 102:2077–2082PubMed CrossRef
  Michalska K, Brzezinski K, Jaskolski M (2005) Crystal structure of isoaspartyl aminopeptidase in complex with l -aspartate. J Biol Chem 280:28484–28491PubMed CrossRef
  Mishra A (2006) Production of l -asparaginase, an anticancer agent, from Aspergillus niger using agricultural waste in solid state fermentation. Appl Biochem Biotechnol 135:33–42PubMed CrossRef
  Nomme J, Su Y, Konrad M, Lavie A (2012) Structures of apo and product-bound human l -asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis. Biochemistry 51:6816–6826PubMed PubMedCentral CrossRef
  Nomme J, Su Y, Lavie A (2014) Elucidation of the specific function of the conserved threonine triad responsible for human L-asparaginase autocleavage and substrate hydrolysis. J Mol Biol 426:2471–2485PubMed PubMedCentral CrossRef
  Pedreschi F, Kaack K, Granby K (2008) The effect of asparaginase on acrylamide formation in French fries. Food Chem 109:386–392PubMed CrossRef
  Roon RJ, Murdoch M, Kunze B, Dunlop PC (1982) Derepression of asparaginase II during exponential growth of Saccharomyces cerevisiae on ammonium ion. Arch Biochem Biophys 219:101–109PubMed CrossRef
  Schalk A, Lavie A (2014) Structural and kinetic characterization of guinea pig l -asparaginase type III. Biochemistry 53:2318–2328PubMed PubMedCentral CrossRef
  Shrivastava A, Khan AA, Khurshid M, Kalam MA, Jain SK, Singhal PK (2015) Recent developments in l -asparaginase discovery and its potential as anticancer agent. Crit Rev Oncol Hematol. doi:10.​1016/​j.​critrevonc.​2015.​01.​002 PubMed
  Su Y, Karamitros CS, Nomme J, McSorley T, Konrad M, Lavie A (2013) Free glycine accelerates the autoproteolytic activation of human asparaginase. Chem Biol 20:533–540PubMed PubMedCentral CrossRef
  Sugimoto H, Odani S, Yamashita S (1998) Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase containing an asparaginase-like region and ankyrin repeat. J Biol Chem 273:12536–12542PubMed CrossRef
  Sun Z, Huang Y, Wang Y, Zhao Y, Cui Z (2014) Potassium hydroxide-ethylene diamine tetraacetic acid method for the rapid preparation of small-scale PCR template DNA from actinobacteria. Mol Genet Microbiol 29:42–46CrossRef
  Sun Z, Lu W, Liu P, Wang H, Huang Y, Zhao Y, Kong Y, Cui Z (2015) Isolation and characterization of a proteinaceous a-amylase inhibitor AAI-CC5 from Streptomyces sp. CC5, and its gene cloning and expression. Antonie Van Leeuwenhoek 107:345–356PubMed CrossRef
  Zuo S, Xue D, Zhang T, Jiang Bo MuW (2014) Biochemical characterization of an extremely thermostable L-asparaginase from Thermococcus gammatolerans EJ3. J Mol Catal B 109:122–129CrossRef
  
• 作者单位：Zhibin Sun (1)
  Ding Li (1)
  Pingping Liu (1)
  Wenhui Wang (1)
  Kai Ji (1)
  Yan Huang (1)
  Zhongli Cui (1)
  
  1. Key Laboratory of Environmental Microbiology of Ministry of Agriculture, Nanjing Agricultural University, Nanjing, 210095, People’s Republic of China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Microbiology
  Medical Microbiology
  Plant Sciences
  Soil Science and Conservation
  
• 出版者：Springer Netherlands
• ISSN：1572-9699

文摘

We have identified a novel l-asparaginase, abASNase3, from Aquabacterium sp. A7-Y. abASNase3 is composed of 306 amino acids and exhibits 34 % sequence homology to human asparaginase (hASNase3). Further analysis revealed that abASNase3 belongs to the N-terminal nucleophile (Ntn) family of hydrolases. Previous reports about the Ntn hydrolase family and the results of our study suggest that abASNase3 must form two subunits by self-cleavage between Gly189 and Thr190 to attain catalytic activity. The two subunits remained tightly associated to build a single functional unit. The optimum pH for abASNase3 was found to be 8.0 in Tris–HCl buffer and the enzyme was found to be stable over a broad pH range from pH 6.0 to 12.0. The optimum temperature for abASNase3 was found to be approximately 40 °C, and the enzyme was stable below 65 °C. abASNase3 showed high substrate specificity toward l-asparagine and had no or only slight activity toward d-asparagine, l-glutamine and d-glutamine. abASNase3 was significantly activated by Mg2+ and was substantially inhibited by Ni2+, Cu2+, Mn2+ and Co2+. The Michaelis–Menten constant and turnover number of abASNase3 for l-asparagine were estimated to be 3.37 × 10−2 M and 8.72 × 10−3 s−1, respectively. Our results indicate that abASNase3 is a novel l-asparaginase in the Ntn family of hydrolases.