C2409
Creatinase from microorganisms
lyophilized powder, ≥4 units/mg solid
Synonyme(s) :
Creatine Amidinohydrolase
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About This Item
Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
bacterial (Actinobacillus spp.)
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥4 units/mg solid
Poids mol.
~100 kDa
Température de stockage
−20°C
Description générale
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.
Application
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.
Actions biochimiques/physiologiques
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.
Propriétés physiques
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)
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)
Définition de l'unité
One unit will hydrolyze 1.0 μmole of creatine to urea and sarcosine per min at pH 7.5 at 37 °C.
Forme physique
Lyophilized powder containing sugars and EDTA as stabilizers
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
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)
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
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
N A Siddiqi et al.
Saudi journal of kidney diseases and transplantation : an official publication of the Saudi Center for Organ Transplantation, Saudi Arabia, 17(2), 203-207 (2006-08-15)
Polyoma virus nephropathy (BK virus) is being recognized as an important cause of graft failure. It is usually confused with acute rejection. No cases have been reported from the kingdom of Saudi Arabia. We report a case of a Saudi
Agnieszka Dzikowska et al.
Fungal genetics and biology : FG & B, 38(2), 175-186 (2003-03-07)
The arginine catabolism gene otaA encoding ornithine transaminase (OTAse) is specifically induced by arginine and is under the control of the broad-domain carbon and nitrogen repression systems. Arginine induction is mediated by a product of arcA gene coding for Zn(2)C(6)
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