Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Microbial enzymes for deprivation of amino acid metabolism in malignant cells: biological strategy for cancer treatment


Amino acid deprivation therapy (AADT) is emerging as a promising strategy for the development of novel therapeutics against cancer. This biological therapy relies upon the differences in the metabolism of cancer and normal cells. The rapid growth of tumors results in decreased expression of certain enzymes leading to auxotrophy for some specific amino acids. These auxotrophic tumors are targeted by amino acid–depleting enzymes. The depletion of amino acid selectively inhibits tumor growth as the normal cells can synthesize amino acids by their usual machinery. The enzymes used in AADT are mostly obtained from microbes for their easy availability. Microbial l-asparaginase is already approved by FDA for the treatment of acute lymphoblastic leukemia. Arginine deiminase and methionase are under clinical trials and the therapeutic potential of lysine oxidase, glutaminase and phenylalanine ammonia lyase is also being explored. The present review provides an overview of microbial amino acid depriving enzymes. Various attributes of these enzymes like structure, mode of action, production, formulations, and targeted cancers are discussed. The challenges faced and the combat strategies to establish AADT in standard cancer armamentarium are also reviewed.

Key Points

• Amino acid deprivation therapy is a potential therapy for auxotrophic tumors.

• Microbial enzymes are used due to their ease of manipulation and high productivity.

• Enzyme properties are improved by PEGylation, encapsulation, and genetic engineering.

• AADT can be employed as combinational therapy for better containment of cancer.

This is a preview of subscription content, log in to check access.

Fig. 1
Fig. 2


  1. Agrawal V, Hee J, Borthakur G, Kantarjian H, Frankel AE (2013) Red blood cell-encapsulated l-asparaginase : potential therapy of patients with asparagine synthetase deficient acute myeloid leukemia. Protein Pept Lett 20:392–402

  2. Ahn J, Choi H, Kim Y, Han KY, Park JS, Han SS, Lee J (2005) Heterologous gene expression using self-assembled supra-molecules with high affinity for HSP70 chaperone. Nucleic Acids Res 33:3751–3762

  3. Ahn KY, Lee B, Han KY, Song JA, Lee DS, Lee J (2014) Synthesis of Mycoplasma arginine deiminase in E. coli using stress-responsive proteins. Enzym Microb Technol 63:46–49

  4. Amano M, Mizuguchi H, Sano T, Kondo H, Shinyashiki K, Inagaki J, Tamura T, Kawaguchi T, Kusakabe H, Imada K, Inagaki K (2015) Recombinant expression, molecular characterization and crystal structure of antitumor enzyme, L-lysine α-oxidase from Trichoderma viride. J Biochem 157(6):549–559

  5. Anastasiou D, Cantley LC (2012) Breathless cancer cells get fat on glutamine. Cell Res 22:443–446

  6. Aung H, Bocola M, Schleper S, Röhm KH (2000) Dynamics of a mobile loop at the active site of Escherichia coli asparaginase. Biochim Biophys Acta 1481:349–359

  7. Avramis VI, Tiwari PN (2006) Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia. Int J Nanomedicine 1(3):241–254

  8. Babich OO, Pokrovsky VS, Anisimova NY, Sokolov NN, Prosekov AY (2013) Recombinant L-phenylalanine ammonia lyase from Rhodosporidium toruloides as a potential anticancer agent. Biotechnol Appl Biochem 60:316–322

  9. Beloussow K, Wang L, Wu J, Ann D, Shen WC (2002) Recombinant arginine deiminase as a potential anti-angiogenic agent. Cancer Lett 183:155–162

  10. Binod P, Sindhu R, Madhavan A, Abraham A, Mathew AK, Beevi US, Sukumaran RK, Singh SP, Pandey A (2017) Recent developments in l-glutaminase production and applications - An overview. Bioresour Technol 245:1766–1774

  11. Borek D, Kozak M, Pei J, Jaskolski M (2014) Crystal structure of active site mutant of antileukemic L -asparaginase reveals conserved zinc-binding site. FEBS J 281:4097–4111

  12. Cachumba JJ, Antunes FA, Peres GF, Brumano LP, Santos JC, Silva SS (2016) Current applications and different approaches for microbial L -asparaginase production. Braz J Microbiol 77–85

  13. Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T (2004) Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry 43(36):11403–11416

  14. Caldwell RB, Toque HA, Narayanan SP, Caldwell RW (2015) Arginase: an old enzyme with new tricks. Trends Pharmacol Sci 36:395–405

  15. Cavuoto P, Fenech MF (2012) A review of methionine dependency and the role of methionine restriction in cancer growth control and life-span extension. Cancer Treat Rev 38:726–736

  16. Cellarier E, Durando X, Vasson M, Farges MC, Demiden A, Maurizis JC, Madelmont JC, Chollet P (2003) Methionine dependency and cancer treatment. Cancer Treat Rev 29:489–499

  17. Cheng PNM, Lam TL, Lam WM, Tsui SM, Cheng AW, Lo WH, Leung YC (2007) Pegylated recombinant human arginase (rhArg-peg5,000 mw) inhibits the in vitro and in vivo proliferation of human hepatocellular carcinoma through arginine depletion. Cancer Res 67:309–317

  18. Crèmel M, Guérin N, Horand F, Banz A, Godfrin Y (2013) Red blood cells as innovative antigen carrier to induce specific immune tolerance. Int J Pharm 443:39–49

  19. Das K, Butler GH, Kwiatkowski V, Clark AD, Yadav P, Arnold E (2004) Crystal structures of arginine deiminase with covalent reaction intermediates : implications for catalytic mechanism. Structure 12:657–667

  20. Delage B, Fennell DA, Nicholson L, McNeish I, Lemoin NR, Crook T, Szlosarek PW (2010) Arginine deprivation and argininosuccinate synthetase expression in the treatment of cancer. Int J Cancer 126:2762–2772

  21. Dhankhar R, Gulati P, Kumar S, Kapoor R (2018) Arginine-lowering enzymes against cancer : a technocommercial analysis through patent landscape. Expert Opin Ther Pat 28:603–614

  22. Dhankhar R, Kumar A, Kumar S, Chhabra D, Shukla P, Gulati P (2019) Multilevel algorithms and evolutionary hybrid tools for enhanced production of arginine deiminase from Pseudomonas furukawaii RS3. Bioresour Technol 290:121789

  23. Dinndorf PA, Gootenberg J, Cohen MH, Keegan P, Pazdur R (2007) FDA drug approval summary: pegaspargase (oncaspar) for the first-line treatment of children with acute lymphoblastic leukemia (ALL). Oncologist 12:991–998

  24. Domenech C, Thomas X, Chabaud S, Baruchel A, Gueyffier F, Mazingue F, Auvrignon A, Corm S, Dombret H, Chevallier P, Galambrun C, Huguet F, Legrand F, Mechinaud F, Vey N, Philip I, Liens D, Godfrin Y, Rigal D, Bertrand Y (2011) L-asparaginase loaded red blood cells in refractory or relapsing acute lymphoblastic leukaemia in children and adults: results of the GRASPALL 2005–01 randomized trial. Br J Haematol 153:58–65

  25. Egler RA, Ahuja SP, Matloub Y (2016) L­asparaginase in the treatment of patients with acute lymphoblastic leukemia. J Pharmacol Pharmacother 7:62–71

  26. El-sayed AS (2010) Microbial L -methioninase : production, molecular characterization, and therapeutic applications. Appl Microbiol Biotechnol 86:445–467

  27. Fayura LR, Boretsky YR, Pynyaha YV, Martynyuk NB, Skorohod VV, Sybyrny АА (2014) Development of cultivation technology for the Escherichia coli recombinant strain producing arginine deiminase of Mycoplasma hominis. Sci Innov 10:29–36

  28. Fernandes HS, Teixeira CSS, Fernandes P, Ramos MJ, Cerqueira NM (2017) Amino acid deprivation using enzymes as a targeted therapy for cancer and viral infections. Expert Opin Ther Pat 27:283–297

  29. Feun L, You M, Wu CJ, Kuo MT, Wangpaichitr M, Spector S, Savaraj N (2008) Arginine deprivation as a targeted therapy for cancer. Int J Cancer 126:2762–2772

  30. Fukumura D, Kashiwagi S, Jain RK (2006) The role of nitric oxide in tumour progression. Nat Rev Cancer 6:521–534

  31. Gerner EW, Meyskens FL (2004) Polyamines and cancer: old molecules, new understanding. Nat Rev Cancer 4:781–792

  32. Gross MI, Demo SD, Dennison JB, Chen L, Chernov-Rogan T, Goyal B, Janes JR, Laidig GJ, Lewis ER, Li J, Mackinnon AL, Parlati F, Rodriguez ML, Shwonek PJ, Sjogren EB, Stanton TF, Wang T, Yang J, Zhao F, Bennett MK (2014) Antitumor activity of the glutaminase inhibitor CB-839 in triple-negative breast cancer. Mol Cancer Ther 13:890–901

  33. Guo L, Wang J, Yan X, Chen R, Qian S, Meng G (2000) Characterization of L -asparaginase fused with a protective ScFv and the protection mechanism. Biochem Biophys Res Commun 203:197–203

  34. Gwangwa MV, Joubert AM, Visagie MH (2019) Effects of glutamine deprivation on oxidative stress and cell survival in breast cell lines. Biol Res 52(1):15

  35. Han RZ, Xu GC, Dong JJ, Ni Y (2016) Arginine deiminase : recent advances in discovery, crystal structure, and protein engineering for improved properties as an anti-tumor drug. Appl Microbiol Biotechnol 100:4747–4760

  36. He H, Ye J, Wang Y, Liu Q, Chung HS, Kwon YM, Shin MC, Lee K, Yang VC (2014) Cell-penetrating peptides meditated encapsulation of protein therapeutics into intact red blood cells and its application. J Control Release 28:123–132

  37. Hens JR, Sinha I, Perodin F, Cooper T, Sinha R, Plummer J, Perrone CE, Orentreich D (2016) Methionine-restricted diet inhibits growth of MCF10AT1-derived mammary tumors by increasing cell cycle inhibitors in athymic nude mice. BMC Cancer 16:349

  38. Hensley CT, Wasti AT, Deberardinis RJ (2013) Glutamine and cancer : cell biology, physiology, and clinical opportunities. J Clin Invest 123:3678–3684

  39. Hoffman RM (2015) Development of recombinant methioninase to target the general cancer-specific metabolic defect of methionine dependence: a 40-year odyssey. Expert Opin Biol Ther 15(1):21–31

  40. Hoffman RM, Tan Y, Li S, Han Q, Zavala J Sr, Zavala J Jr (2019) Pilot Phase I clinical trial of methioninase on high-stage cancer patients: rapid depletion of circulating methionine. Methods Mol Biol 1866:231–242

  41. Hori H, Takabayashi K, Orvis L, Carson DA, Nobori T (1996) Gene cloning and characterization of Pseudomonas putida L-Methionine-α- deamino-γ-mercaptomethane-lyase. Cancer Res 56:2116–2122

  42. Jacque N, Bouscary D (2014) Targeting glutamine uptake in AML. Oncoscience 1:1–2

  43. Jeon H, Kim JH, Lee E, Jang YJ, Son JE, Kwon JY, Lim TG, Kim S, Park JH, Kim JE, Lee KW (2016) Methionine deprivation suppresses triple-negative breast cancer metastasis in vitro and in vivo. Oncotarget 7:67223–67234

  44. Jiang H, Huang K, Mu W, Jiang B, Zhang T (2018) Characterization of a recombinant arginine deiminase from Enterococcus faecalis SK32.001 for L-citrulline production. Process Biochem 64:136–142

  45. Knott SRV, Wagenblast E, Khan S, Kim SY, Soto M, Wagner M, Turgeon MO, Fish L, Erard N, Gable AL, Maceli AR, Dickopf S, Papachristou EK, D’Santos CS, Carey LA, Wilkinson JE, Harrell JC, Perou CM, Goodarzi H, Poulogiannis G, Hannon GJ (2018) Asparagine bioavailability governs metastasis in a model of breast cancer. Nature 554:378–381

  46. Kozai M, Sasamori E, Fujihara M, Yamashita T, Taira H, Harasawa R (2009) Growth inhibition of human melanoma cells by a recombinant arginine deiminase expressed in Escherichia coli. J Vet Med Sci 71:1343–1347

  47. Krupyanko VI, Medentsev AG, Lukasheva EV, Arinbasarova AY (2017) Kinetic characteristics of L-lysine α- oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D: Substrate specificity and allosteric effects. Biochem and Biophys Reports 9:9–12

  48. Kudou D, Misaki S, Yamashita M, Tamura T, Takakura T, Yoshioka T, Yagi S, Hoffman RM, Takimoto A, Esaki N, Inagaki K (2007) Structure of the antitumour enzyme L -Methionine c-Lyase from Pseudomonas putida at 1.8 A°. J Biochem 544:535–544

  49. Kulis M, Esteller M (2010) DNA methylation and cancer. Adv Genet 70:27–56

  50. Kuo MT, Savaraj N, Feun LG (2010) Targeted cellular metabolism for cancer chemotherapy with recombinant arginine-degrading enzymes. Oncotarget 1:246–251

  51. Kusakabe H, Kodama K, Kuninaka A, Yoshino H, Misono H, Soda K (1980) Effect of L- lysine α--oxidase on growth of mouse leukemic cells. Agric Biol Chem 44:387–392

  52. Lukasheva EV, Berezov TT (2002) L-Lysine α oxidase : physicochemical and biological properties. Biochemistry (Mosc) 67:1152–1158

  53. Lukey MJ, Wilson KF, Cerione RA (2013) Therapeutic strategies impacting cancer cell glutamine metabolism. Future Med Chem 5:1685–1700

  54. MacDonald MJ, D’Cunha GB (2007) A modern view of phenylalanine ammonia lyase. Biochem Cell Biol 85:273–282

  55. Mahajan RV, Saran S, Kameswaran K, Kumar V, Saxena RK (2012) Efficient production of l-asparaginase from Bacillus licheniformis with low-glutaminase activity: optimization, scaleup and acrylamide degradation studies. Bioresour Technol 125:11–16

  56. Mcguire S (2016) World cancer report 2014. Geneva, Switzerland : World Health Organization, International Agency for Research on Cancer, WHO Press, 2015. Adv Nutr 7:418–9

  57. Mishra P, Nayak B, Dey RK (2016) PEGylation in anti-cancer therapy: an overview. Asian J Pharm Sci 11:337–348

  58. Miyazaki K, Takaku H, Umeda M, Fujita T, Huang WD, Kimura T, Yamashita J, Horio T (1990) Potent growth inhibition of human tumor cells in culture by arginine deiminase purified from a culture medium of a Mycoplasma-infected cell line. Cancer Res 50:4522–4527

  59. Naidu MU, Ramana GV, Rani PU, Mohan IK, Suman A, Roy P (2004) Chemotherapy-induced and / or radiation therapy -induced oral mucositis — complicating the treatment of cancer. Neoplasia 6:423–431

  60. Nandakumar R, Yoshimune K, Wakayama M, Moriguchi M (2003) Microbial glutaminase: biochemistry, molecular approaches and applications in the food industry. J Mol Catal B Enzym 23:87–100

  61. Ni Y, Schwaneberg U, Sun ZH (2008) Arginine deiminase, a potential anti-tumor drug. Cancer Lett 261(1):1–11

  62. Pandian SRK, Deepak V, Sivasubramaniam SD, Nellaiah H, Sundar K (2014) Optimization and purification of anticancer enzyme L-glutaminase from Alcaligenes faecalis KLU102. Biologia (Bratisl) 69:1644–1651

  63. Pasut G, Sergi M (2008) Anti-cancer PEG-enzymes: 30 years old, but still a current approach. Adv Drug Deliv Res 60:69–78

  64. Patil M, Bhaumik J, Babykutty S, Banerjee UC, Fukumura D (2016) Arginine dependence of tumor cells: targeting a chink in cancer’s armor. Oncogene 35:4957–4972

  65. Pham JV, Yilma MA, Feliz A, Majid MT, Maffetone N, Walker JR, Kim E, Cho HJ, Reynolds JM, Song MC, Park SR, Yoon YJ (2019) A review of the microbial production of bioactive natural products and biologics. Front Microbiol 10:1404

  66. Pokrovsky VS, Treshalina HM, Lukasheva EV, Sedakova LA, Medentzev AG, Arinbasarova AY, Berezov TT (2013) Enzymatic properties and anticancer activity of L-lysine α-oxidase from Trichoderma cf. aureoviride Rifai BKMF-4268D. Anti-Cancer Drugs 24:846–851

  67. Proud CG (2014) Control of the translational machinery by amino acids. Am J Clin Nutr 99:231–236

  68. Rohde T, MacLean D, Klarlund PB (1996) Glutamine, lymphocyte proliferation and cytokine production. Scand J Immunol 44:648–650

  69. Schulenburg C, Ardelt B, Ardelt W, Arnold U, Shogen K, Ulbrich-Hofmann R, Darzynkiewicz Z (2007) The interdependence between catalytic activity, conformational stability, and cytotoxicity of onconase. Cancer Biol Ther 6:1233–1239

  70. Selim MH, Elshikh HH, Saad MM, Mostafa EE, Mahmoud MA (2016) Purification and characterization of a novel thermo stable L-methioninase from Streptomyces sp. DMMMH4 and its evaluation for anticancer activity. J Appl Pharm Sci 6:53–60

  71. Sharma B, Singh S, Kanwar SS (2014) L-Methionase: a therapeutic enzyme to treat malignancies. Biomed Res Int 2014:506287

  72. Shrivastava A, Khan AA, Khurshid M, Kalam MA, Jain SK, Singhal PK (2016) Recent developments in l-asparaginase discovery and its potential as anticancer agent. Crit Rev Oncol Hematol 100:1–10

  73. Singh P, Banik RM (2013) Biochemical characterization and antitumor study of L-glutaminase from Bacillus cereus MTCC 1305. Appl Biochem Biotechnol 171:522–531

  74. Song J, Lee D, Park J, Han KY, Lee J (2011) A novel Escherichia coli solubility enhancer protein for fusion expression of aggregation-prone heterologous proteins. Enzym Microb Technol 49:124–130

  75. Song P, Ye L, Fan J, Li Y, Zeng X, Wang Z, Wang S, Zhang G, Yang P, Cao Z, Ju D (2015) Asparaginase induces apoptosis and cytoprotective autophagy in chronic myeloid leukemia cells. Oncotarget 6:3861–3873

  76. Spiers AS, Wade HE (1976) Bacterial glutaminase in treatment of acute leukemia. Br Med J 1:1317–1319

  77. Strekalova E, Malin D, Hoelper D, Lewi P, Cryns V (2018) Targeting methionine metabolism to eradicate cancer stem cells. Proceedings: AACR Annual Meeting; April 14–18, 2018; Chicago

  78. Strohl WR (2015) Fusion proteins for half-life extension of biologics as a strategy to make biobetters. BioDrugs 29:215–239

  79. Suganya K, Govindan K, Prabha P, Murugan M (2017) An extensive review on L-methioninase and its potential applications. Biocatal Agric Biotechnol 12:104–115

  80. Sun X, Yang Z, Li S, Tan Y, Zhang N, Wang X (2003) In vivo efficacy of recombinant methioninase is enhanced by the combination of polyethylene glycol conjugation and pyridoxal 5 ′ -phosphate supplementation. Cancer Res 63:8377–8383

  81. Tabe Y, Lorenzi PL, Konopleva M (2019) Amino acid metabolism in hematologic malignancies and the era of targeted therapy. Blood 134:1014–1023

  82. Tan Y, Zavala J Sr, Xu M, Zavala J Jr, Hoffman RM (1996) Serum methionine depletion without side effects by methioninase in metastatic breast cancer patients. Anticancer Res 16:3937–3942

  83. Turecek PL, Bossard MJ, Schoetens F, Ivens IA (2016) PEGylation of biopharmaceuticals: a review of chemistry and nonclinical safety information of approved drugs. J Pharm Sci 105:460–475

  84. Unissa R, Sudhakar M, Reddy ASK, Sravanthi KN (2014) A review on biochemical and therapeutic aspects of glutaminase. Int J Pharm Sci Res 5:4617–4634

  85. Wang J, Erickson JW, Fuji R, Ramachandran S, Gao P, Dinavahi R, Wilson KF, Ambrosio AL, Dias SM, Dang CV, Cerione RA (2010) Targeting mitochondrial glutaminase activity inhibits oncogenic transformation. Cancer Cell 18:207–219

  86. Wang T, Hsia S, Shieh T (2017) Lysyl oxidase and the tumor micro environment. Int J Mol Sci 18:62

  87. Wheatley DN, Campbell E (2002) Arginine catabolism, liver extracts and cancer. Pathol Oncol Res 8:18–25

  88. Wong SHK, Goode DL, Iwasaki M, Wei MC, Kuo HP, Zhu L, Schneidawind D, Duque-Afonso J, Weng Z, Cleary ML (2015) The H3K4-methyl epigenome regulates leukemia stem cell oncogenic potential. Cancer Cell 28:198–209

  89. Wu G (2009) Amino acids: Metabolism, functions, and nutrition. Amino Acids 37:1–17

  90. Wu G (2013) Functional amino acids in nutrition and health. Amino Acids 45:407–411

  91. Xiong L, Teng JLL, Botelho MG, Lo RC, Lau SK, Woo PC (2016) Arginine metabolism in bacterial pathogenesis and cancer therapy. Int J Mol Sci 17:363–381

  92. Yang J, Tao R, Wang L, Song L, Wang Y, Gong C, Yao S, Wu Q (2019) Thermosensitive micelles encapsulating phenylalanine ammonia lyase act as a sustained and efficacious therapy against colorectal cancer. J Biomed Nanotechnol 15:717–727

  93. Yang Z, Wang J, Yoshioka T, Li B, Lu Q, Li S, Sun X, Tan Y, Yagi S, Frenkel EP, Hoffman RM (2004) Pharmacokinetics, methionine depletion, and antigenicity of recombinant methioninase in primates. Clin Cancer Res 10:2131–2138

  94. Yau T, Cheng PN, Chan P, Chan W, Chen L, Yuen J (2013) A phase 1 dose-escalating study of pegylated recombinant human arginase 1 (Peg-rhArg1) in patients with advanced hepatocellular carcinoma. Investig New Drugs 1:99–107

  95. You M, Savaraj N, Kuo MT, Wangpaichitr M, Varona-Santos J, Wu C (2013) TRAIL induces autophagic protein cleavage through caspase activation in melanoma cell lines under arginine deprivation. Mol Cell Biochem 374:181–190

  96. Zhang L, Liu M, Jamil S, Han R, Xu G, Ni Y (2015) PEGylation and pharmacological characterization of a potential anti-tumor drug, an engineered arginine deiminase originated from Pseudomonas plecoglossicida. Cancer Lett 357:346–354

  97. Zhu L, Verma R, Roccatano D, Ni Y, Sun ZH, Schwaneberg U (2010) A potential antitumor drug (arginine deiminase) reengineered for efficient operation under physiological conditions. Chem Bio Chem 11:2294–2301

  98. Zion market research report (2016) Cancer drugs market by therapy (immunotherapy, targeted therapy, chemotherapy, hormone therapy and others) for breast cancer, blood cancer, gastrointestinal cancer, prostate cancer, skin cancer, lung cancer and other cancer: global industry perspective, Co. 2016

  99. Zou S, Wang X, Liu P, Ke C, Xu S (2019) Arginine metabolism and deprivation in cancer therapy. Biomed Pharmacother 118:109210

Download references


RD is grateful to the Department of Science and Technology-Science and Engineering Research Board (DST-SERB) and MDU, Rohtak, for providing the fellowship. The authors thank DST for providing FIST grant (1196 SR/FST/LS-I/2017/4) for the development of infrastructural facilities.


This study was financially supported by DST-SERB (SB/YS/LS-145/2014).

Author information

PG conceived and designed the layout of the manuscript. RD and PG carried out the literature survey. RD and VG wrote the manuscript. SK and RKK prepared the figures. PG critically analyzed and revised the manuscript. All authors read and approved the manuscript.

Correspondence to Pooja Gulati.

Ethics declarations

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

Conflict of interest

The authors declare they have no conflict of interest.

Additional information

Publisher’s note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and Permissions

About this article

Verify currency and authenticity via CrossMark

Cite this article

Dhankhar, R., Gupta, V., Kumar, S. et al. Microbial enzymes for deprivation of amino acid metabolism in malignant cells: biological strategy for cancer treatment. Appl Microbiol Biotechnol (2020).

Download citation


  • Anti-cancerous enzymes
  • Anti-tumor enzymes
  • Amino acid deprivation therapy
  • Auxotrophic tumors
  • Biological cancer treatment
  • PEGylation