Application | Comment | Organism |
---|---|---|
analysis | biomatrix fabricated to investigate immobilization of creatine amidinohydrolase | Actinobacillus sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.5 | - |
Creatine | parameter calculated for the bioelectrode, depends on the electrode material and the enzyme immobilization process, indicates that nanocomposite matrix has a high affinity to immobilize CAH enzyme, the small Km value indicates a high enzyme affinity to the nanocomposite matrix over the electrode surface, attributed to the advantageous nanoporous surface for the enzyme immobilization that can favor conformational changes of the enzyme, also attributed to high surface-to-volume ratio, which can help to effectively immobilize the enzyme onto the nanocomposite | Actinobacillus sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
creatine + H2O | Actinobacillus sp. | - |
sarcosine + urea | - |
? | |
creatine + H2O | Actinobacillus sp. CRH-211 | - |
sarcosine + urea | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Actinobacillus sp. | Q7SIB5 | - |
- |
Actinobacillus sp. CRH-211 | Q7SIB5 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
biomatrix fabricated to investigate immobilization of creatine amidinohydrolase, characterized with Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM) and cyclic voltammetry (CV), enzyme affinity to the nanocomposite matrix estimated using the Hanes plot, photometric study to calculate the apparent enzyme activity, influence of various parameters on enzyme activity within the matrix analyzed including pH, temperature, time | Actinobacillus sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
creatine + H2O | - |
Actinobacillus sp. | sarcosine + urea | - |
? | |
creatine + H2O | biomatrix fabricated to investigate immobilization of creatine amidinohydrolase | Actinobacillus sp. | sarcosine + urea | - |
? | |
creatine + H2O | - |
Actinobacillus sp. CRH-211 | sarcosine + urea | - |
? | |
creatine + H2O | biomatrix fabricated to investigate immobilization of creatine amidinohydrolase | Actinobacillus sp. CRH-211 | sarcosine + urea | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CAH | - |
Actinobacillus sp. |
Creatine amidinohydrolase | - |
Actinobacillus sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
33 | - |
optimum temperature range calculated between 32 and 34°C | Actinobacillus sp. |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
26 | 43 | optimum temperature range calculated between 32 and 34°C due to the increased kinetic energy of the reacting molecules, current of the bioelectrode measured at different temperatures ranging from 26 to 43°C in the presence of creatine 150 microM and a phosphate buffer (50 mM, pH 7.0) | Actinobacillus sp. |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
26 | 43 | thermal stability of the bioelectrode studied by measuring the current at different temperatures ranging from 26 to 43°C in the presence of creatine at 150 microM and a phosphate buffer (50 mM, pH 7.0) | Actinobacillus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
optimum of enzyme activity attributed to the potential positive influence of the dehydrated chitosan on the enzyme activity, suggests that chitosan-SiO2-multiwall carbon nanotubes nanocomposite matrix is suitable for enzyme applications at neutral condition | Actinobacillus sp. |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | electrode matrix suitable for enzyme applications at neutral condition | Actinobacillus sp. |