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Literature summary extracted from

  • Berberich, J.A.; Yang, L.W.; Bahar, I.; Russell, A.J.
    A stable three enzyme creatinine biosensor. 2. Analysis of the impact of silver ions on creatine amidinohydrolase (2005), Acta Biomater., 1, 183-191.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.3.3 medicine creatinine determination in biological fluids Actinobacillus sp.

General Stability

EC Number General Stability Organism
3.5.3.3 stability of creatine amidinohydrolase-containing polyurethane hydrogels stored in buffer at 37°C decreases after 1 week, PEGylation of creatine-amidinohydrolase leads to decrease of half-life when stored in buffer at 37°C Actinobacillus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.3 AgNO3
-
Actinobacillus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.3.3 45000
-
-
Actinobacillus sp.

Organism

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

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
-
Actinobacillus sp. CRH-211 sarcosine + urea
-
?

Subunits

EC Number Subunits Comment Organism
3.5.3.3 homodimer
-
Actinobacillus sp.

Synonyms

EC Number Synonyms Comment Organism
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 37
-
-
Actinobacillus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.3.3 7.5
-
-
Actinobacillus sp.