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Literature summary for 3.5.3.6 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
Search for more literature for 3.5.3.6

Application

Application Comment Organism
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

General Stability Organism
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
the resistance of the enzyme conjugated with dextran to proteolysis is increased by 2.5folds to proteinase K and trypsin Aspergillus nidulans

Inhibitors

Inhibitors Comment Organism Structure
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
AlCl3 1 mM, dextran-conjugated enzyme and native enzyme retain 47% and 48% of their initial activities Aspergillus nidulans
BaCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 61.2% and 58.8% of their initial activities Aspergillus nidulans
CaCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 45.9% and 51.9% of their initial activities Aspergillus nidulans
CuSO4 1 mM, dextran-conjugated enzyme and native enzyme retain 33% and 43.4% of their initial activities Aspergillus nidulans
DTNB 1 mM, dextran-conjugated enzyme and native enzyme retain 46.7% and 4.9% of their initial activities Aspergillus nidulans
FeCl3 1 mM, dextran-conjugated enzyme and native enzyme retain 45% and 50% of their initial activities Aspergillus nidulans
H2O2 1 mM, dextran-conjugated enzyme and native enzyme retain 25.8% and 2.9% of their initial activities Aspergillus nidulans
HgCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 40% and 13.4% of their initial activities Aspergillus nidulans
hydroxylamine 1 mM, dextran-conjugated enzyme and native enzyme retain 24.5% and 2.3% of their initial activities Aspergillus nidulans
iodoacetate 1 mM, dextran-conjugated enzyme and native enzyme retain 23.9% and 2.6% of their initial activities Aspergillus nidulans
K2CrO4 1 mM, dextran-conjugated enzyme and native enzyme retain 42% and 36% of their initial activities Aspergillus nidulans
KCl 1 mM, dextran-conjugated enzyme and native enzyme retain 97% and 98% of their initial activities Aspergillus nidulans
MBTH 1 mM, dextran-conjugated enzyme and native enzyme retain 20.5% and 2.6% of their initial activities Aspergillus nidulans
MgCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 49% and 14.3% of their initial activities Aspergillus nidulans
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
Na2WO4 1 mM, dextran-conjugated enzyme and native enzyme retain 30% and 26.9% of their initial activities Aspergillus nidulans
NaCl 1 mM, dextran-conjugated enzyme and native enzyme retain 13% and 11% of their initial activities Aspergillus nidulans
NaIO3 1 mM, dextran-conjugated enzyme and native enzyme retain 41% and 34% of their initial activities Aspergillus nidulans
PMSF 1 mM, dextran-conjugated enzyme and native enzyme retain 1.1% and 1.2% of their initial activities Aspergillus nidulans
Urea 1 mM, dextran-conjugated enzyme and native enzyme retain 46.5% and 36% of their initial activities Aspergillus nidulans
ZnCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 12% and 10% of their initial activities Aspergillus nidulans

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aspergillus nidulans

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
ADI
-
 Aspergillus nidulans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
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]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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

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