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Literature summary for 4.4.1.1 extracted from
- Biochemical and pharmacokinetic properties of PEGylated cystathionine gamma-lyase from Aspergillus carneus KF723837 (2015), J. Mol. Microbiol. Biotechnol., 25, 301-310 .
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | covalent binding of enzyme to polyethylene glycol moieties reduces the specific activity from 59.71 U/mg of free enzyme to 48.71 U/mg, with a PEGylation yield of 81.5 and 70.7% modification of surface epsilon-amino groups. The pH stability does not change upon modification, and at 50 ° C, the thermal stability of PEG-CGL is increased by 40% in comparison to free CGL. By in vitro proteolysis, PEG-CGL retains more than 50% of its initial activity compared to less than 10% of the free-CGL for acid protease for 30 min. The biochemical and hematological responses of rabbits indicate nil toxicity of free and PEG-CGL | Aspergillus carneus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 6-diazo-5-oxonorleucine | - |
Aspergillus carneus |  |
| iodoacetate | - |
Aspergillus carneus | |
| propargylglycine | - |
Aspergillus carneus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.36 | - |
DL-cystathionine | native enzyme, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | |
| 3.4 | - |
DL-cystathionine | protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 204000 | - |
PAGE | Aspergillus carneus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus carneus | - |
- |
- |
| Aspergillus carneus KF723837 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purification by various chromatographic approaches | Aspergillus carneus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 48.71 | - |
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus |
| 59.71 | - |
native enzyme, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DL-cystathionine + H2O | - |
Aspergillus carneus | L-cysteine + 2-oxobutanoate + NH3 | - |
? | |
| DL-cystathionine + H2O | - |
Aspergillus carneus KF723837 | L-cysteine + 2-oxobutanoate + NH3 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 52000, SDS-PAGE | Aspergillus carneus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
half-life of free enzyme 5.31 h, of PEG-CGL 9.01 h, respectively | Aspergillus carneus |
| 40 | - |
half-life of free enzyme 2.78 h, of PEG-CGL 3.1 h, respectively | Aspergillus carneus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.11 | - |
DL-cystathionine | protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | |
| 0.13 | - |
DL-cystathionine | native enzyme, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.66 | - |
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | iodoacetate | |
| 0.91 | - |
native enzyme, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | propargylglycine | |
| 0.98 | - |
native enzyme, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | iodoacetate | |
| 1.34 | - |
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | 6-diazo-5-oxonorleucine | |
| 1.49 | - |
protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | propargylglycine | |
| 2.16 | - |
native enzyme, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | 6-diazo-5-oxonorleucine | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.029 | - |
DL-cystathionine | protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | |
| 0.04 | - |
DL-cystathionine | native enzyme, pH not specified in the publication, temperature not specified in the publication | Aspergillus carneus | |
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