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Literature summary extracted from

  • Tiwari, A.; Dhakate, S.R.
    Chitosan-SiO2-multiwall carbon nanotubes nanocomposite: a novel matrix for the immobilization of creatine amidinohydrolase (2009), Int. J. Biol. Macromol., 44, 408-412.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.3.3 analysis biomatrix fabricated to investigate immobilization of creatine amidinohydrolase Actinobacillus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.3 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.3.3 creatine + H2O Actinobacillus sp.
-
 sarcosine + urea
-
 ?
3.5.3.3 creatine + H2O Actinobacillus sp. CRH-211
-
 sarcosine + urea
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.3 Actinobacillus sp. Q7SIB5
-
-
3.5.3.3 Actinobacillus sp. CRH-211 Q7SIB5
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.3.3 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.3 creatine + H2O
-
 Actinobacillus sp. sarcosine + urea
-
 ?
3.5.3.3 creatine + H2O biomatrix fabricated to investigate immobilization of creatine amidinohydrolase Actinobacillus sp. sarcosine + urea
-
 ?
3.5.3.3 creatine + H2O
-
 Actinobacillus sp. CRH-211 sarcosine + urea
-
 ?
3.5.3.3 creatine + H2O biomatrix fabricated to investigate immobilization of creatine amidinohydrolase Actinobacillus sp. CRH-211 sarcosine + urea
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.3.3 CAH
-
 Actinobacillus sp.
3.5.3.3 Creatine amidinohydrolase
-
 Actinobacillus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.3.3 33
-
 optimum temperature range calculated between 32 and 34°C Actinobacillus sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.3.3 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 [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.3.3 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.3.3 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 Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.3.3 6 8 electrode matrix suitable for enzyme applications at neutral condition Actinobacillus sp.