Cat No.
DIA-185
Description
In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction: creatine + H2O ?sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism.
Abbr
Creatinase, Native (Microorganism)
Alias
Creatinase
Species
Microorganism
Form
Freeze dried powder
Enzyme Commission Number
EC 3.5.3.3
Bio-activity
GradeⅡ 4.0 U/mg-solid or more
Appearance
White amorphous powder, lyophilized
Molecular Mass
approx. 67 kDa (by gel filtration)
pH Stability
pH 4.0-10.0 (25°C, 20hr)
Michaelis Constant
4.5×10－3 M (Creatine)
Structure
2 subunits per mol of enzyme
Isoelectric point
4.5±0.1
Optimum pH
6.5-7.5
Optimum temperature
40－50°C
Stabilizers
Sugars, EDTA
Thermal stability
below 70°C (pH 7.5, 30min)
Stability
Stable at -20°C for at least one year
Inhibitors
Hg??, Cu??, Ag?, SH reagent (NEM), PCMB
Applications
This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis.
Synonyms
Creatine amidohydrolase; Creatinase; EC 3.5.3.3
