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Merck

C2409

Sigma-Aldrich

Creatinase from microorganisms

lyophilized powder, ≥4 units/mg solid

Synonym(e):

Creatine Amidinohydrolase

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About This Item

CAS-Nummer:
EC-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

bacterial (Actinobacillus spp.)

Form

lyophilized powder

Spezifische Aktivität

≥4 units/mg solid

Mol-Gew.

~100 kDa

Lagertemp.

−20°C

Allgemeine Beschreibung

Creatinase is a homodimer that catalyzes hydrolysis of creatine. It consists of two monomer subunits and two defined domains; N and C terminal domains. The C-terminal fold has both the α helices and anti-parallel β sheet within two structurally similar domains.In between these two domains, a sulfhydryl group acts as active site, and the activity is metal-independent.

Anwendung

Creatinase mixed with sarcosine oxidase may be used to determine the level of creatine in different pH, temperature, enzyme ratio, and buffer concentration. It may also be used to determine the plasma creatinine level by using a centrifugal analyser.

Biochem./physiol. Wirkung

Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride.

Physikalische Eigenschaften

Isoelectric point: 4.6 ± 0.1
Michaelis constant: 1.9 x 10‾2M (Creatine)
Structure: 2 subunits per mole of enzyme
Inhibitors: Cu++, Hg++, Ag+
Optimum pH: 8.0
Optimum temp: 40°C
pH Stability: pH 5.5 − 9.0 (25°C, 16hr)
Thermal stability: Below 50°C (pH 7.5, 30 min)

Einheitendefinition

One unit will hydrolyze 1.0 μmole of creatine to urea and sarcosine per min at pH 7.5 at 37 °C.

Physikalische Form

Lyophilized powder containing sugars and EDTA as stabilizers

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Balasundaram Padmanabhan et al.
Acta crystallographica. Section D, Biological crystallography, 58(Pt 8), 1322-1328 (2002-07-24)
The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4)
H Crocker et al.
Journal of clinical pathology, 41(5), 576-581 (1988-05-01)
An enzymatic kit method for the determination of plasma creatinine was optimised for use with a centrifugal analyser and its performance characteristics and practicability compared with an end point and a kinetic Jaffé-based method. The enzymatic method exhibited several advantages
J F Bazan et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(7), 2473-2477 (1994-03-29)
Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C-terminal domain of Pseudomonas putida creatinase (EC 3.5.3.3) are related. A detailed comparison of the three-dimensional folds of the two enzymes confirms this
Pinar Esra Erden et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 34(2), 223-239 (2006-03-16)
A new enzyme electrode for the determination of creatine was developed by immobilizing creatinase (CI) and sarcosine oxidase (SO). The enzymes were co-immobilized in a poly(vinylferrocenium) matrix onto the surface of a platinum working electrode. Crosslinking with glutaraldehyte (GA) and
Jason A Berberich et al.
Acta biomaterialia, 1(2), 183-191 (2006-05-17)
The enzyme creatine amidinohydrolase is a clinically important enzyme used in the determination of creatinine in blood and urine. Continuous use biosensors are becoming more important in the clinical setting; however, long-use creatinine biosensors have not been commercialized due to

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