Structural and kinetic characterization of guinea pig l-asparaginase type III

Biochemistry

Volumn 53, Issue 14, 2014, Pages 2318-2328

  Schalk, Amanda M ^a   Lavie, Arnon ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BODY FLUIDS; DISEASES; ENZYME ACTIVITY; PROTEINS;

ACUTE LYMPHOBLASTIC LEUKEMIA; ANTI-CANCER AGENTS; BACTERIAL ENZYMES; KINETIC CHARACTERIZATION; MICHAELIS CONSTANTS; MICROMOLAR RANGE; MILLIMOLAR RANGE; SERENDIPITOUS DISCOVERY;

MAMMALS;

AMINO ACID SEQUENCE; ANIMALS; ASPARAGINASE; CATALYTIC DOMAIN; CLONING, MOLECULAR; GUINEA PIGS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84898890486     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401692v     Document Type: Article

References (57)

1. Kidd, J. G. (1953) Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum J. Exp. Med. 98, 565-582
2. Broome, J. D. (1961) Evidence that the L-asparaginase activity of guinea pig serum is responsible for its antilymphoma effects Nature 191, 1114-1115
3. Broome, J. D. (1963) 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, 99-120
4. Mashburn, L. T. and Wriston, J. C., Jr. (1964) Tumor inhibitory effect of L-asparaginase from Escherichia coli Arch. Biochem. Biophys. 105, 450-452
5. Wade, H. E., Robinson, H. K., and Phillips, B. W. (1971) Asparaginase and glutaminase activities of bacteria J. Gen. Microbiol. 69, 299-312
6. Ertel, I. J., Nesbit, M. E., Hammond, D., Weiner, J., and Sather, H. (1979) Effective dose of L-asparaginase for induction of remission in previously treated children with acute lymphocytic leukemia: a report from Childrens Cancer Study Group Cancer Res. 39, 3893-3896
7. Cooney, D. A., Capizzi, R. L., and Handschumacher, R. E. (1970) Evaluation of L-asparagine metabolism in animals and man Cancer Res. 30, 929-935
8. Haley, E. E., Fischer, G. A., and Welch, A. D. (1961) The requirement for L-asparagine of mouse leukemia cells L5178Y in culture Cancer Res. 21, 532-536
9. Neuman, R. E. and McCoy, T. A. (1956) Dual requirement of Walker carcinosarcoma 256 in vitro for asparagine and glutamine Science 124, 124-125
10. Muller, H. J. and Boos, J. (1998) Use of L-asparaginase in childhood ALL Crit. Rev. Oncol./Hematol. 28, 97-113
11. Avramis, V. I. and Tiwari, P. N. (2006) Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia Int. J. Nanomed. 1, 241-254
12. Ahlke, E., Nowak-Gottl, U., Schulze-Westhoff, P., Werber, G., Borste, H., Wurthwein, G., Jurgens, H., and Boos, J. (1997) Dose reduction of asparaginase under pharmacokinetic and pharmacodynamic control during induction therapy in children with acute lymphoblastic leukaemia Br. J. Haematol. 96, 675-681
13. Asselin, B. L., Whitin, J. C., Coppola, D. J., Rupp, I. P., Sallan, S. E., and Cohen, H. J. (1993) Comparative pharmacokinetic studies of three asparaginase preparations J. Clin. Oncol. 11, 1780-1786
14. Abuchowski, A., van Es, T., Palczuk, N. C., McCoy, J. R., and Davis, F. F. (1979) Treatment of L5178Y tumor-bearing BDF1 mice with a nonimmunogenic L-glutaminase-L-asparaginase Cancer Treat. Rep. 63, 1127-1132
15. Abuchowski, A., Kazo, G. M., Verhoest, C. R., Jr., Van Es, T., Kafkewitz, D., Nucci, M. L., Viau, A. T., and Davis, F. F. (1984) Cancer therapy with chemically modified enzymes. I. Antitumor properties of polyethylene glycol-asparaginase conjugates Cancer Biochem. Biophys. 7, 175-186
16. Pasut, G. and Veronese, F. M. (2009) PEG conjugates in clinical development or use as anticancer agents: an overview Adv. Drug Delivery Rev. 61, 1177-1188
17. Keating, M. J., Holmes, R., Lerner, S., and Ho, D. H. (1993) L-asparaginase and PEG asparaginase - past, present, and future Leuk. Lymphoma 10 (Suppl) 153-157
18. Armstrong, J. K., Hempel, G., Koling, S., Chan, L. S., Fisher, T., Meiselman, H. J., and Garratty, G. (2007) Antibody against poly(ethylene glycol) adversely affects PEG-asparaginase therapy in acute lymphoblastic leukemia patients Cancer 110, 103-111
19. Muller, H. J., Loning, L., Horn, A., Schwabe, D., Gunkel, M., Schrappe, M., von Schutz, V., Henze, G., Casimiro da Palma, J., Ritter, J., Pinheiro, J. P., Winkelhorst, M., and Boos, J. (2000) Pegylated asparaginase (Oncaspar) in children with ALL: drug monitoring in reinduction according to the ALL/NHL-BFM 95 protocols Br. J. Haematol. 110, 379-384
20. Avramis, V. I. and Panosyan, E. H. (2005) Pharmacokinetic/pharmacodynamic relationships of asparaginase formulations: the past, the present and recommendations for the future Clin. Pharmacokinet. 44, 367-393
21. Boos, J., Werber, G., Ahlke, E., Schulze-Westhoff, P., Nowak-Gottl, U., Wurthwein, G., Verspohl, E. J., Ritter, J., and Jurgens, H. (1996) Monitoring of asparaginase activity and asparagine levels in children on different asparaginase preparations Eur. J. Cancer 32A, 1544-1550
22. Dellinger, C. T. and Miale, T. D. (1976) Comparison of anaphylactic reactions to asparaginase derived from Escherichia coli and from Erwinia cultures Cancer 38, 1843-1846
23. Muller, H. J., Beier, R., da Palma, J. C., Lanvers, C., Ahlke, E., von Schutz, V., Gunkel, M., Horn, A., Schrappe, M., Henze, G., Kranz, K., and Boos, J. (2002) PEG-asparaginase (Oncaspar) 2500 U/m(2) BSA in reinduction and relapse treatment in the ALL/NHL-BFM protocols Cancer Chemother. Pharmacol. 49, 149-154
24. UniProt, C. (2013) Update on activities at the Universal Protein Resource (UniProt) in 2013 Nucleic Acids Res. 41, D43-47
25. Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Soding, J., Thompson, J. D., and Higgins, D. G. (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega Mol. Syst. Biol. 7, 539
26. Bush, L. A., Herr, J. C., Wolkowicz, M., Sherman, N. E., Shore, A., and Flickinger, C. J. (2002) A novel asparaginase-like protein is a sperm autoantigen in rats Mol. Reprod. Dev. 62, 233-247
27. Cantor, J. R., Stone, E. M., Chantranupong, L., and Georgiou, G. (2009) The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity Biochemistry 48, 11026-11031
28. Evtimova, V., Zeillinger, R., Kaul, S., and Weidle, U. H. (2004) Identification of CRASH, a gene deregulated in gynecological tumors Int. J. Oncol. 24, 33-41
29. Borek, D., Michalska, K., Brzezinski, K., Kisiel, A., Podkowinski, J., Bonthron, D. T., Krowarsch, D., Otlewski, J., and Jaskolski, M. (2004) Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog Eur. J. Biochem. 271, 3215-3226
30. Michalska, K., Brzezinski, K., and Jaskolski, M. (2005) Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate J. Biol. Chem. 280, 28484-28491
31. Michalska, K., Bujacz, G., and Jaskolski, M. (2006) Crystal structure of plant asparaginase J. Mol. Biol. 360, 105-116
32. Nomme, J., Su, Y., Konrad, M., and Lavie, A. (2012) Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis Biochemistry 51, 6816-6826
33. Prahl, A., Pazgier, M., Hejazi, M., Lockau, W., and Lubkowski, J. (2004) Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli Acta Crystallogr., Sect. D 60, 1173-1176
34. Su, Y., Karamitros, C. S., Nomme, J., McSorley, T., Konrad, M., and Lavie, A. (2013) Free glycine accelerates the autoproteolytic activation of human asparaginase Chem. Biol. 20, 533-540
35. Brannigan, J. A., Dodson, G., Duggleby, H. J., Moody, P. C., Smith, J. L., Tomchick, D. R., and Murzin, A. G. (1995) A protein catalytic framework with an N-terminal nucleophile is capable of self-activation Nature 378, 416-419
36. Hejazi, M., Piotukh, K., Mattow, J., Deutzmann, R., Volkmer-Engert, R., and Lockau, W. (2002) Isoaspartyl dipeptidase activity of plant-type asparaginases Biochem. J. 364, 129-136
37. Larsen, R. A., Knox, T. M., and Miller, C. G. (2001) Aspartic peptide hydrolases in Salmonella enterica serovar typhimurium J. Bacteriol. 183, 3089-3097
38. Fernandez, C. A., Cai, X., Elozory, A., Liu, C., Panetta, J. C., Jeha, S., Molinelli, A. R., and Relling, M. V. (2013) High-throughput asparaginase activity assay in serum of children with leukemia Int. J. Clin. Exp. Med. 6, 478-487
39. Kabsch, W. (2010) Xds Acta Crystallogr., Sect. D 66, 125-132
40. Vagin, A. and Teplyakov, A. (2010) Molecular replacement with MOLREP Acta Crystallogr., Sect. D 66, 22-25
41. Padilla, J. E. and Yeates, T. O. (2003) A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning Acta Crystallogr., Sect. D 59, 1124-1130
42. Adams, P. D., Afonine, P. V., Bunkoczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., McCoy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution Acta Crystallogr., Sect. D 66, 213-221
43. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr., Sect. D 53, 240-255
44. Zheng, H., Chordia, M. D., Cooper, D. R., Chruszcz, M., Muller, P., Sheldrick, G. M., and Minor, W. (2014) Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server Nat. Protoc. 9, 156-170
45. Emsley, P., Lohkamp, B., Scott, W. G., and Cowtan, K. (2010) Features and Development of Coot Acta Crystallogr., Sect. D 66, 486-501
46. Borek, D. and Jaskolski, M. (2000) Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome Acta Crystallogr., Sect. D 56, 1505-1507
47. Aswad, D. W., Paranandi, M. V., and Schurter, B. T. (2000) Isoaspartate in peptides and proteins: formation, significance, and analysis J. Pharm. Biomed. Anal. 21, 1129-1136
48. Oinonen, C. and Rouvinen, J. (2000) Structural comparison of Ntn-hydrolases Protein Sci. 9, 2329-2337
49. Wang, Y. and Guo, H. C. (2010) Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing J. Mol. Biol. 403, 120-130
50. Laskowski, R. A., Hutchinson, E. G., Michie, A. D., Wallace, A. C., Jones, M. L., and Thornton, J. M. (1997) PDBsum: a Web-based database of summaries and analyses of all PDB structures Trends Biochem. Sci. 22, 488-490
51. Duggleby, H. J., Tolley, S. P., Hill, C. P., Dodson, E. J., Dodson, G., and Moody, P. C. (1995) Penicillin acylase has a single-amino-acid catalytic centre Nature 373, 264-268
52. Lowe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., and Huber, R. (1995) Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution Science 268, 533-539
53. Aronson, N. N., Jr. (1996) Lysosomal glycosylasparaginase: a member of a family of amidases that employ a processed N-terminal threonine, serine or cysteine as a combined base-nucleophile catalyst Glycobiology 6, 669-675
54. Guan, C., Liu, Y., Shao, Y., Cui, T., Liao, W., Ewel, A., Whitaker, R., and Paulus, H. (1998) Characterization and functional analysis of the cis-autoproteolysis active center of glycosylasparaginase J. Biol. Chem. 273, 9695-9702
55. Michalska, K., Borek, D., Hernandez-Santoyo, A., and Jaskolski, M. (2008) Crystal packing of plant-type L-asparaginase from Escherichia coli Acta Crystallogr., Sect. D 64, 309-320
56. Michalska, K., Hernandez-Santoyo, A., and Jaskolski, M. (2008) The mechanism of autocatalytic activation of plant-type L-asparaginases J. Biol. Chem. 283, 13388-13397
57. Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis, Nat. Methods 9, 671-675.