F7296
Fructosyl-Amino Acid Oxidase from Corynebacterium sp.
recombinant, expressed in E. coli, lyophilized powder, ≥0.45 units/mg protein
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About This Item
Numéro de classification (Commission des enzymes):
1.5.3.x
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥0.45 units/mg protein
Poids mol.
~88 kDa by electrophoresis
Température de stockage
−20°C
Description générale
Fructosyl amino acid oxidase [fructosyl-a-l-amino acid:oxygen oxidoreductase] is a flavoprotein that catalyzes the oxidation of fructosyl amino acids to form glucosone, amino acid and hydrogen peroxide.
Enzyme Commission (E.C.) 1.5.3.x
Application
Fructosyl-Amino Acid Oxidase from Corynebacterium sp has been used in glycated haemoglobin HbA1c detection in blood samples using quartz crystal microbalance (QCM) based detection.
Fructosyl-amino acid oxidase can be used to detect the levels of glycated proteins, which are markers for diabetes mellitus.
Actions biochimiques/physiologiques
Fructosamines are formed when glucose is condensed amino group of amino acids or proteins. Fructosamine oxidases (FAOX) catalyze the oxidative deglycation of low molecular weight fructosamines. Fructosyl amino acid oxidase catalyzes the oxidation of the C-N bond linking the C1 of the fructosyl moiety and the nitrogen of the amino group of fructosyl amino acids.
Fructosyl-Amino Acid Oxidase (FAOD) comprises of FAD-binding motifs and is classified into three types based on substrate specificity. The engineered Corynebacterium Fructosyl-Amino Acid Oxidase is stable at 45°C and could be exploited for the development of glycated protein biosensing system and glycated hemoglobin HbA1c measurements. FAOD shares sequence homology with fructosyl peptide oxidase and both are effective on α-fructosyl substrates.
Suitable for the determination of fructosyl-L-amino acid.
Définition de l'unité
One unit will produce 1.0 μmole of hydrogen peroxide per minute at pH 8.0 at 37 °C.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
S A Schellini et al.
Acta ophthalmologica, 67(5), 601-604 (1989-10-01)
The authors report a case of fibrohistiocytoma of the limbus and discuss the clinical, histopathological and immunohistochemical findings concerning this type of lesion, with a comparison of their findings with those reported in the literature.
Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum.
M. Fujiwara et al.
Applied Microbiology, 74, 813-819 (2007)
Y Sakai et al.
FEBS letters, 459(2), 233-237 (1999-10-13)
A high-level production of fructosyl amino acid oxidase (FAOD), whose production was toxic in Escherichia coli, was investigated through attempts to utilize the peroxisome of Candida boidinii as the place for protein accumulation. The alcohol oxidase-depleted strain (strain aod1Delta) produced
C Gerhardinger et al.
The Journal of biological chemistry, 270(1), 218-224 (1995-01-06)
A Pseudomonas sp. soil strain, selected for its ability to grow on epsilon-(1-deoxyfructosyl) aminocaproic acid, was induced to express a membrane-bound enzymatic activity which oxidatively degrades Amadori products into free fructosamine. Apparent Km values for fructosyl aminocaproate, epsilon-fructosyl lysine, fructosyl
Structural basis of the substrate specificity of the FPOD/FAOD family revealed by fructosyl peptide oxidase from Eupenicillium terrenum
Gan W, et al.
Acta Crystallographica. Section F, Structural Biology Communications, 71(4), 381-387 (2015)
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