1. Dhankhar R, Gupta V, Kumar S, Kapoor RK, Gulati P. Microbial enzymes for deprivation of amino acid metabolism in malignant cells: biological strategy for cancer treatment. Appl Microbiol Biotechnol. 2020;104(7):2857-2869. doi:10.1007/s00253-020-10432-2
2. Han RZ, Xu GC, Dong JJ, Ni Y. Arginine deiminase: recent advances in discovery, crystal structure, and protein engineering for improved properties as an anti-tumor drug. Appl Microbiol Biotechnol. 2016;100(11):4747-4760. doi:10.1007/s00253-016-7490-z
3. Maneerat K, Yongkiettrakul S, Jiemsup S, Tongtawe P, Gottschalk M, Srimanote P. Expression and characterization of serotype 2 Streptococcus suis arginine deiminase. Microb Physiol. 2017;27(3):133-146. doi:10.1159/000452952
4. Zúñiga M, Pérez G, González-Candelas F. Evolution of arginine deiminase (ADI) pathway genes. Mol Phylogenet Evol. 2002;25(3):429-444. doi:10.1016/S1055-7903(02)00277-4
5. Dhankhar R, Gulati P, Kumar S, Kapoor RK. Arginine-lowering enzymes against cancer: a technocommercial analysis through patent landscape. Expert Opin Ther Pat. 2018;28(8):603-614. doi:10.1080/13543776.2018.1508452
6. Riess C, Shokraie F, Classen CF, et al. Arginine-depleting enzymes – an increasingly recognized treatment strategy for therapy-refractory malignancies. Cell Physiol Biochem. 2018;51(2):854-870. doi:10.1159/000495382
7. Patil MD, Bhaumik J, Babykutty S, Banerjee UC, Fukumura D. Arginine dependence of tumor cells: targeting a chink in cancer’s armor. Oncogene. 2016;35(38):4957-4972. doi:10.1038/onc.2016.37
8. Shen LJ, Beloussow K, Shen WC. Modulation of arginine metabolic pathways as the potential anti-tumor mechanism of recombinant arginine deiminase. Cancer Lett. 2006;231(1):30-35. doi:10.1016/j.canlet.2005.01.007
9. Kawatra A, Dhankhar R, Gulati P. Microbial arginine deiminase: a multifaceted green catalyst in biomedical sciences. Int J Biol Macromol. 2022;196:151-162. doi:10.1016/j.ijbiomac.2021.12.015
10. Kuo MT, Savaraj N, Feun LG. Targeted cellular metabolism for cancer chemotherapy with recombinant arginine-degrading enzymes. Oncotarget. 2010;1(4):246-251. Accessed January 4, 2022. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2998341/
11. Abou-Alfa GK, Qin S, Ryoo BY, et al. Phase III randomized study of second line ADI-PEG 20 plus best supportive care versus placebo plus best supportive care in patients with advanced hepatocellular carcinoma. Ann Oncol. 2018;29(6):1402-1408. doi:10.1093/annonc/mdy101
12. Yang TS, Lu SN, Chao Y, et al. A randomised phase II study of pegylated arginine deiminase (ADI-PEG 20) in Asian advanced hepatocellular carcinoma patients. Br J Cancer. 2010;103(7):954-960. doi:10.1038/sj.bjc.6605856
13. Armstrong JK, Hempel G, Koling S, et al. Antibody against poly(ethylene glycol) adversely affects PEG-asparaginase therapy in acute lymphoblastic leukemia patients. Cancer. 2007;110(1):103-111. doi:10.1002/cncr.22739
14. Sherman MR, Saifer MGP, Perez-Ruiz F. PEG-uricase in the management of treatment-resistant gout and hyperuricemia. Adv Drug Deliv Rev. 2008;60(1):59-68. doi:10.1016/j.addr.2007.06.011
15. Dhankhar R, Kumar A, Kumar S, Chhabra D, Shukla P, Gulati P. Multilevel algorithms and evolutionary hybrid tools for enhanced production of arginine deiminase from Pseudomonas furukawaii RS3. Bioresour Technol. 2019;290:121789. doi:10.1016/j.biortech.2019.121789
16. Kimura N, Watanabe T, Suenaga H, et al. Pseudomonas furukawaii sp. nov., a polychlorinated biphenyl-degrading bacterium isolated from biphenyl-contaminated soil in Japan. Int J Syst Evol Microbiol. 2018;68(5):1429-1435. doi:10.1099/ijsem.0.002670
17. Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987;4(4):406-425. doi:10.1093/oxfordjournals.molbev.a040454
18. Kumar S, Stecher G, Li M, Knyaz C, Tamura K. MEGA X: molecular evolutionary genetics analysis across computing platforms. Mol Biol Evol. 2018;35(6):1547-1549. doi:10.1093/molbev/msy096
19. Felsenstein J. Confidence limits on phylogenies: an approach using the bootstrap. Evol Int J Org Evol. 1985;39(4):783-791. doi:10.1111/j.1558-5646.1985.tb00420.x
20. Nei M, Kumar S. Molecular Evolution and Phylogenetics. Oxford University Press; 2000.
21. Doytchinova IA, Flower DR. VaxiJen: a server for prediction of protective antigens, tumour antigens and subunit vaccines. BMC Bioinformatics. 2007;8(1):4. doi:10.1186/1471-2105-8-4
22. Saha S, Raghava GPS. AlgPred: prediction of allergenic proteins and mapping of IgE epitopes. Nucleic Acids Res. 2006;34(suppl_2):W202-W209. doi:10.1093/nar/gkl343
23. Gonzalez-Galarza FF, Christmas S, Middleton D, Jones AR. Allele frequency net: a database and online repository for immune gene frequencies in worldwide populations. Nucleic Acids Res. 2011;39(suppl_1):D913-D919. doi:10.1093/nar/gkq1128
24. Southwood S, Sidney J, Kondo A, et al. Several common hla-dr types share largely overlapping peptide binding repertoires. J Immunol. 1998;160(7):3363-3373. Accessed January 4, 2022. https://www.jimmunol.org/content/160/7/3363
25. Kringelum JV, Lundegaard C, Lund O, Nielsen M. Reliable B cell epitope predictions: impacts of method development and improved benchmarking. PLOS Comput Biol. 2012;8(12):e1002829. doi:10.1371/journal.pcbi.1002829
26. Sweredoski MJ, Baldi P. PEPITO: improved discontinuous B-cell epitope prediction using multiple distance thresholds and half sphere exposure. Bioinformatics. 2008;24(12):1459-1460. doi:10.1093/bioinformatics/btn199
27. Angelis MD, Mariotti L, Rossi J, et al. Arginine catabolism by sourdough lactic acid bacteria: purification and characterization of the arginine deiminase pathway enzymes from Lactobacillus sanfranciscensis CB1. Appl Environ Microbiol. Published online December 2002. doi:10.1128/AEM.68.12.6193-6201.2002
28. Qian J, Sun Z, Liu Y, Meng F, Liu Y. Determination of L-citrulline in enzymatic conversion solution by diacetylmonoxime-thiosemicarbazide colorimetry. Chin. J. Pharm. 2007;38:519–522.
29. Bala K, Husain I, Sharma A. Arginine deaminase from Pseudomonas aeruginosa PS2: purification, biochemical characterization and in-vitro evaluation of anticancer activity. 3 Biotech. 2020;10(5):226. doi:10.1007/s13205-020-02212-6
30. Liu YM, Sun ZH, Ni Y, Zheng P, Liu YP, Meng FJ. Isolation and identification of an arginine deiminase producing strain Pseudomonas plecoglossicida CGMCC2039. World J Microbiol Biotechnol. 2008;24(10):2213-2219. doi:10.1007/s11274-008-9732-4
31. Ni Y, Li Z, Sun Z, et al. Expression of arginine deiminase from Pseudomonas plecoglossicida CGMCC2039 in Escherichia coli and its anti-tumor activity. Curr Microbiol. 2009;58(6):593-598. doi:10.1007/s00284-009-9376-0
32. Zarei M, Nezafat N, Rahbar MR, et al. Decreasing the immunogenicity of arginine deiminase enzyme via structure-based computational analysis. J Biomol Struct Dyn. 2019;37(2):523-536. doi:10.1080/07391102.2018.1431151
33. Evander Emeltan Tjoa S, Maria Vianney Y, Emantoko Dwi Putra S. In silico mutagenesis: decreasing the immunogenicity of botulinum toxin type A. J Biomol Struct Dyn. 2019;37(18):4767-4778. doi:10.1080/07391102.2018.1559100
34. Belén LH, Lissabet JB, de Oliveira Rangel-Yagui C, et al. A structural in silico analysis of the immunogenicity of l-asparaginase from Escherichia coli and Erwinia carotovora. Biologicals. 2019;59:47-55. doi:10.1016/j.biologicals.2019.03.003
35. Tripathi S, Parmar J, Kumar A. Structure-based immunogenicity prediction of uricase from fungal (Aspergillus flavus), bacterial (Bacillus subtillis) and mammalian sources using immunoinformatic approach. Protein J. 2020;39(2):133-144. doi:10.1007/s10930-020-09886-0
36. Liu W, Peng Z, Liu Z, Lu Y, Ding J, Chen YH. High epitope density in a single recombinant protein molecule of the extracellular domain of influenza A virus M2 protein significantly enhances protective immunity. Vaccine. 2004;23(3):366-371. doi:10.1016/j.vaccine.2004.05.028
37. Egler RA, Ahuja SP, Matloub Y. L-asparaginase in the treatment of patients with acute lymphoblastic leukemia. J Pharmacol Pharmacother. 2016;7(2):62. doi:10.4103/0976-500X.184769
38. Jiang H, Huang K, Mu W, Jiang B, Zhang T. Characterization of a recombinant arginine deiminase from Enterococcus faecalis SK32.001 for L-citrulline production. Process Biochem. 2018;64:136-142. doi:10.1016/j.procbio.2017.06.006
39. Kim JE, Jeong DW, Lee HJ. Expression, purification, and characterization of arginine deiminase from Lactococcus lactis ssp. lactis ATCC 7962 in Escherichia coli BL21. Protein Expr Purif. 2007;53(1):9-15. doi:10.1016/j.pep.2006.12.002
40. Misawa S, Aoshima M, Takaku H, Matsumoto M, Hayashi H. High-level expression of Mycoplasma arginine deiminase in Escherichia coli and its efficient renaturation as an anti-tumor enzyme. J Biotechnol. 1994;36(2):145-155. doi:10.1016/0168-1656(94)90050-7
41. Ni Y, Schwaneberg U, Sun ZH. Arginine deiminase, a potential anti-tumor drug. Cancer Lett. 2008;261(1):1-11. doi:10.1016/j.canlet.2007.11.038
42. Oudjama Y, Tricot C, Stalon V, Wouters J. Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa L-arginine deiminase. Acta Crystallogr D Biol Crystallogr. 2002;58(12):2150-2152. doi:10.1107/S0907444902015743
43. Lu X, Li L, Wu R, et al. Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function. Biochemistry. 2006;45(4):1162-1172. doi:10.1021/bi051591e
44. Patil MD, Rathod VP, Bihade UR, Banerjee UC. Purification and characterization of arginine deiminase from Pseudomonas putida: structural insights of the differential affinities of L-arginine analogues. J Biosci Bioeng. 2019;127(2):129-137. doi:10.1016/j.jbiosc.2018.07.021
45. Ni Y, Liu Y, Schwaneberg U, et al. Rapid evolution of arginine deiminase for improved anti-tumor activity. Appl Microbiol Biotechnol. 2011;90(1):193-201. doi:10.1007/s00253-010-3051-z
46. Ensor CM, Holtsberg FW, Bomalaski JS, Clark MA. Pegylated arginine deiminase (ADI-SS PEG20,000 mw) inhibits human melanomas and hepatocellular carcinomas in vitro and in vivo. Cancer Res. 2002;62(19):5443-5450.
47. Kozai M, Sasamori E, Fujihara M, Yamashita T, Taira H, Harasawa R. Growth inhibition of human melanoma cells by a recombinant arginine deiminase expressed in Escherichia coli. J Vet Med Sci. 2009;71(10):1343-1347. doi:10.1292/jvms.001343
48. McAlpine JA, Lu HT, Wu KC, Knowles SK, Thomson JA. Down-regulation of argininosuccinate synthetase is associated with cisplatin resistance in hepatocellular carcinoma cell lines: implications for PEGylated arginine deiminase combination therapy. BMC Cancer. 2014;14(1):621. doi:10.1186/1471-2407-14-621