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Literature summary extracted from

  • El-Sayed, A.; Shindia, A.; Zeid, A.; Yassin, A.; Sitohy, M.; Sitohy, B.
    Aspergillus nidulans thermostable arginine deiminase-Dextran conjugates with enhanced molecular stability, proteolytic resistance, pharmacokinetic properties and anticancer activity (2019), Enzyme Microb. Technol., 131, 109432 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.3.6 drug development 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 Aspergillus nidulans

General Stability

EC Number General Stability Organism
3.5.3.6 dextran-enzyme conjugates exhibit a higher thermal stability by about 2folds for all the tested temperatures, ensuring the acquired structural and catalytic stability upon dextran conjugation Aspergillus nidulans
3.5.3.6 the resistance of the enzyme conjugated with dextran to proteolysis is increased by 2.5folds to proteinase K and trypsin Aspergillus nidulans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.6 6-diazo-5-oxo-norleucine 1 mM, dextran-conjugated enzyme and native enzyme retain 10.1% and 1.5% of their initial activities Aspergillus nidulans
3.5.3.6 AlCl3 1 mM, dextran-conjugated enzyme and native enzyme retain 47% and 48% of their initial activities Aspergillus nidulans
3.5.3.6 BaCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 61.2% and 58.8% of their initial activities Aspergillus nidulans
3.5.3.6 CaCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 45.9% and 51.9% of their initial activities Aspergillus nidulans
3.5.3.6 CuSO4 1 mM, dextran-conjugated enzyme and native enzyme retain 33% and 43.4% of their initial activities Aspergillus nidulans
3.5.3.6 DTNB 1 mM, dextran-conjugated enzyme and native enzyme retain 46.7% and 4.9% of their initial activities Aspergillus nidulans
3.5.3.6 FeCl3 1 mM, dextran-conjugated enzyme and native enzyme retain 45% and 50% of their initial activities Aspergillus nidulans
3.5.3.6 H2O2 1 mM, dextran-conjugated enzyme and native enzyme retain 25.8% and 2.9% of their initial activities Aspergillus nidulans
3.5.3.6 HgCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 40% and 13.4% of their initial activities Aspergillus nidulans
3.5.3.6 hydroxylamine 1 mM, dextran-conjugated enzyme and native enzyme retain 24.5% and 2.3% of their initial activities Aspergillus nidulans
3.5.3.6 iodoacetate 1 mM, dextran-conjugated enzyme and native enzyme retain 23.9% and 2.6% of their initial activities Aspergillus nidulans
3.5.3.6 K2CrO4 1 mM, dextran-conjugated enzyme and native enzyme retain 42% and 36% of their initial activities Aspergillus nidulans
3.5.3.6 KCl 1 mM, dextran-conjugated enzyme and native enzyme retain 97% and 98% of their initial activities Aspergillus nidulans
3.5.3.6 MBTH 1 mM, dextran-conjugated enzyme and native enzyme retain 20.5% and 2.6% of their initial activities Aspergillus nidulans
3.5.3.6 MgCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 49% and 14.3% of their initial activities Aspergillus nidulans
3.5.3.6 additional information dextran conjugation slightly protects the reactive amino and thiols groups of surface amino acids of the enzyme from amino acids suicide inhibitors Aspergillus nidulans
3.5.3.6 Na2WO4 1 mM, dextran-conjugated enzyme and native enzyme retain 30% and 26.9% of their initial activities Aspergillus nidulans
3.5.3.6 NaCl 1 mM, dextran-conjugated enzyme and native enzyme retain 13% and 11% of their initial activities Aspergillus nidulans
3.5.3.6 NaIO3 1 mM, dextran-conjugated enzyme and native enzyme retain 41% and 34% of their initial activities Aspergillus nidulans
3.5.3.6 PMSF 1 mM, dextran-conjugated enzyme and native enzyme retain 1.1% and 1.2% of their initial activities Aspergillus nidulans
3.5.3.6 Urea 1 mM, dextran-conjugated enzyme and native enzyme retain 46.5% and 36% of their initial activities Aspergillus nidulans
3.5.3.6 ZnCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 12% and 10% of their initial activities Aspergillus nidulans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.6 0.92
-
 L-arginine pH 8.0, 37°C, dextran-conjugated enzyme Aspergillus nidulans
3.5.3.6 4.8
-
 L-arginine pH 8.0, 37°C, soluble enzyme Aspergillus nidulans
3.5.3.6 9.5
-
 Boc-Gln-Arg-Arg-MCA pH 8.0, 37°C, dextran-conjugated enzyme Aspergillus nidulans
3.5.3.6 12.3
-
 Boc-Gln-Arg-Arg-MCA pH 8.0, 37°C, soluble enzyme Aspergillus nidulans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.3.6 K+ dependency on K+ ions as a cofactor Aspergillus nidulans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.3.6 120000
-
-
 Aspergillus nidulans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.3.6 L-arginine + H2O Aspergillus nidulans
-
 L-citrulline + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.6 Aspergillus nidulans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.3.6
-
 Aspergillus nidulans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.3.6 12.9
-
 pH 8.0, 37°C Aspergillus nidulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.6 Boc-Gln-Arg-Arg-MCA + H2O
-
 Aspergillus nidulans ? + NH3
-
 ?
3.5.3.6 L-arginine + H2O
-
 Aspergillus nidulans L-citrulline + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.3.6 heterotrimer 3 * 48000, SDS-PAGE Aspergillus nidulans

Synonyms

EC Number Synonyms Comment Organism
3.5.3.6 ADI
-
 Aspergillus nidulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.3.6 37
-
 native enzyme and enzyme conjugated with dextran via the epsilon-amino groups interaction of surface lysine residues of the enzyme Aspergillus nidulans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.3.6 4
-
 soluble enzyme (t1/2: 1445 h), dextran-conjugated enzyme (t1/2: 2440 h) Aspergillus nidulans
3.5.3.6 30
-
 soluble enzyme (t1/2: 23.5 h), dextran-conjugated enzyme (t1/2: 40.2 h) Aspergillus nidulans
3.5.3.6 37
-
 soluble enzyme (t1/2: 17.3 h), dextran-conjugated enzyme (t1/2: 34.2 h) Aspergillus nidulans
3.5.3.6 45
-
 soluble enzyme (t1/2: 3.4 h), dextran-conjugated enzyme (t1/2: 8.4 h) Aspergillus nidulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.3.6 7 8 native enzyme and enzyme conjugated with dextran via the epsilon-amino groups interaction of surface lysine residues of the enzyme Aspergillus nidulans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.3.6 6 9.5 pH 6.0: about 50% of maximal activity, pH 9.5: about 55% of maximal activity, soluble enzyme Aspergillus nidulans