3.5.3.6: arginine deiminase
This is an abbreviated version!
For detailed information about arginine deiminase, go to the full flat file.
Word Map on EC 3.5.3.6
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3.5.3.6
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ornithine
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streptococcus
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argininosuccinate
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pegylated
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levan
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king
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carbamate
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reisolated
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mycoplasma
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water-soaked
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syringae
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greenhouse
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urease
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arginase
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adi-peg20
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lopat
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dna-dna
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melibiose
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pathovars
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d-sorbitol
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midi
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gordonii
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l-citrulline
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voges-proskauer
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newark
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l-rhamnose
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symptomless
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aesculin
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d-mannitol
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rep-pcr
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ncppb
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surface-sterilized
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lecithinase
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glistening
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cichorii
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amygdalin
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arginine-dependent
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supragingival
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deimination
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phytopathology
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sanguinis
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non-spore-forming
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salicin
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malolactic
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maculicola
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monterey
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dulcitol
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caries-free
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hayward
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drug development
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adonitol
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pharmacology
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synthesis
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medicine
- 3.5.3.6
- ornithine
- streptococcus
- argininosuccinate
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pegylated
- levan
-
king
- carbamate
-
reisolated
- mycoplasma
-
water-soaked
- syringae
-
greenhouse
- urease
- arginase
-
adi-peg20
-
lopat
-
dna-dna
- melibiose
-
pathovars
- d-sorbitol
-
midi
- gordonii
- l-citrulline
-
voges-proskauer
-
newark
- l-rhamnose
-
symptomless
- aesculin
- d-mannitol
-
rep-pcr
-
ncppb
-
surface-sterilized
- lecithinase
-
glistening
- cichorii
- amygdalin
-
arginine-dependent
-
supragingival
-
deimination
-
phytopathology
- sanguinis
-
non-spore-forming
- salicin
-
malolactic
- maculicola
-
monterey
- dulcitol
-
caries-free
-
hayward
- drug development
- adonitol
- pharmacology
- synthesis
- medicine
Reaction
Synonyms
ADI, ArcA, arcA-1, arcA-2, arginine deiminase, arginine dihydrolase, arginine-degrading enzyme, citrulline iminase, deiminase, arginine, L-arginine deiminase, LADI, lymphocyte blastogenesis inhibitory factor, More, PaADI, PAD, PAD2, peptidylarginine deiminase, PpADI, Streptococcal acid glycoprotein
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Application on EC 3.5.3.6 - arginine deiminase
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drug development
medicine
pharmacology
synthesis
additional information
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ADI is a potential anti-tumor drug for the treatment of argine-auxotrophic tumors, e.g. hepatocellular carcinoma and melanoma
drug development
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ADI is a potential anti-tumor drug for the treatment of argine-auxotrophic tumors, e.g. hepatocellular carcinoma and melanoma
drug development
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ADI is a potential anti-tumor drug for the treatment of argine-auxotrophic tumors, e.g. hepatocellular carcinoma and melanoma
drug development
arginine deiminase is a therapeutic protein for cancer therapy of arginine-auxotrophic tumors. An ammonia detection-based screening system for arginine deiminase activity improvement at low arginine concentrations is developed and validated by identifying variants of the Pseudomonas plecoglossicida arginine deiminase with improved activity at physiological arginine concentrations. Four amino acid substitutions are identified to reduce S0.5 values or increase kcat values. The antiproliferation activity of the improved enzyme variant K30R/C37R/L148P/V291L is investigated and compared to wild-type and mutant enzyme K5T/D38H/D44E/A128T/E296K/H404R by in vitro experiments with two relevant melanoma cell lines under physiological conditions. Pseudomonas plecoglossicida arginine deiminase variant K30R/C37R/L148P/V291L is a highly attractive candidate to be used as therapeutic protein for the treatment of arginine-auxotrophic melanomas
drug development
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L-arginine deiminase has a powerful anticancer activity against various tumors, via arginine depletion, arresting the cell cycle at G1 phase. The free and PEGylated enzyme exhibits a similar cytotoxic efficacy against HCT, HEP-G2, and MCF7 cells, lower than the cytotoxic efficacy of to enzyme covalently immobilized on dextran. The in vitro anticancer activity of the enzyme against HCT, MCF7, and HEPG-2 cells is increased by five-, three-, and threefold upon covalent modification by dextran
drug development
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possibility of a use of the enzyme as a potential anticancer drug. Purified enzyme exhibits profound antiproliferative activity against Hep-G2 cells. Purified enzyme induces apoptosis in the Hep-G2 cells by DNA fragmentation
drug development
the enzyme is a particularly attractive therapeutic target for breast cancer because it is recruited by the estrogen receptor to endoplasmic reticulum target gene promoters where it citrullinates histone H3 at R26, leading to ER-target gene activation
drug development
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the enzyme shows potential anticancer activity against various arginine-auxotrophic tumors. The higher antigenicity, structural instability and in vivo proteolysis are the major challenges that limit this enzyme from further clinical implementation. The anticancer activity of the enzyme to breast (MCF-7), liver (HepG-2) and colon (HCT8, HT29, DLD1 and LS174 T) cancer cell lines is increased by 1.7folds with dextran conjugation in vitro. Pharmacokinetically, the half-life time of ADI is increased by 1.7folds upon dextran conjugation, in vivo. From the biochemical and hematological parameters, arginine deiminase has no signs of toxicity to the experimental animals
drug development
the lack of this enzyme in the human host makes arginine deiminase an attractive target for drug design against Giardia intestinalis
drug development
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possibility of a use of the enzyme as a potential anticancer drug. Purified enzyme exhibits profound antiproliferative activity against Hep-G2 cells. Purified enzyme induces apoptosis in the Hep-G2 cells by DNA fragmentation
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drug development
Aspergillus fumigatus KJ434941
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L-arginine deiminase has a powerful anticancer activity against various tumors, via arginine depletion, arresting the cell cycle at G1 phase. The free and PEGylated enzyme exhibits a similar cytotoxic efficacy against HCT, HEP-G2, and MCF7 cells, lower than the cytotoxic efficacy of to enzyme covalently immobilized on dextran. The in vitro anticancer activity of the enzyme against HCT, MCF7, and HEPG-2 cells is increased by five-, three-, and threefold upon covalent modification by dextran
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possibility of a future use of arginine deiminase for the therapy of leukemia. The enzyme is 100fold more potent in inhibiting the proliferation of cultured human lymphatic leukemia cell lines while it appears to be less effective in leukemia cells of myeloid origin
medicine
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arginine deiminase is a chemotherapeutic agent against arginine-requiring tumours and has potential application in antiviral therapy (suppressive factor of HIV-1 replication)
medicine
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arginine deiminase conjugated to PEG 20 000 reduces extracellular arginine, has minimal toxicity, decreases tumor burden and improves liver function in patients with chronic hepatitis C virus infection and inoperable hepatocellular carcinoma, overview
medicine
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arginine deprivation by arginine deiminase I can provide a beneficial strategy for the treatment of pancreatic cancer
medicine
the recombinant enzyme can effectively inhibit H22 tumor growth at a total dose of 5 U/mouse over a 2-week dosing period
medicine
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the recombinant enzyme has a potentially therapeutic role in inducible nitric oxide synthase-related neuronal diseases
medicine
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pegylated ADI is a promising drug that capitalizes on a significant enzymatic deficiency in human hepatocellular carcinoma
medicine
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the enzyme has potential for the suppression of excessive cell proliferation
medicine
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the recombinant enzyme can effectively inhibit H22 tumor growth at a total dose of 5 U/mouse over a 2-week dosing period
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medicine
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the enzyme has potential for the suppression of excessive cell proliferation
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ADI has anti-cancer activity by causing depletion of L-arginine, fusion of ADI to 20 kDa PEG improves its pharmaceutical efficiency by increasing the half-life of the enzyme in serum, clinical studies, overview
pharmacology
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ADI is a potential anti-angiogenic agent and is effective in the treatment of leukemia, ADI in clinical studies, overview
pharmacology
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ADI is a potential anti-angiogenic agent and is effective in the treatment of leukemia, ADI in clinical studies, overview
pharmacology
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ADI is a potential anti-angiogenic agent and is effective in the treatment of leukemia, ADI in clinical studies, overview
L-citrulline can be enzymatically produced by arginine deiminase
synthesis
Enterococcus faecalis SK23.001
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L-citrulline can be enzymatically produced by arginine deiminase
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human serum albumin is an effective fusion partner for chemically modifying the enzyme resulting in a longer half-life in serum of two weeks, human serum albumin is more suitable than PEG, overview
additional information
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PEG binding does not affect the enzyme activity, but does improve pharmocodynamics and pharmacokinetics, best at 20 kDa size of PEG, overview