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 | 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 | 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 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 | Comment | Organism | Structure |
---|---|---|---|
K+ | dependency on K+ ions as a cofactor | Aspergillus nidulans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
120000 | - |
- |
Aspergillus nidulans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine + H2O | Aspergillus nidulans | - |
L-citrulline + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus nidulans | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Aspergillus nidulans |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
12.9 | - |
pH 8.0, 37°C | Aspergillus nidulans |
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 | Comment | Organism |
---|---|---|
heterotrimer | 3 * 48000, SDS-PAGE | Aspergillus nidulans |
Synonyms | Comment | Organism |
---|---|---|
ADI | - |
Aspergillus nidulans |
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 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 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 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 |