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A6941

Sigma-Aldrich

Alcohol Oxidase from Candida boidinii

lyophilized powder, 5-15 units/mg protein

Synonyme(s) :

AOD1, AOX, Alcohol:oxygen oxidoreductase

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About This Item

Numéro CAS:
9073-63-6
Numéro de classification (Commission des enzymes):
1.1.3.13 (BRENDA, IUBMB)
Numéro CE :
232-971-3
Numéro MDL:
MFCD00130452
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

fungus (Candida boidinii)

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

5-15 units/mg protein

Poids mol.

octomer 600 kDa by sedimentation equilibrium

Solubilité

100 mM potassium phosphate, pH 7.5: soluble 1.0 mg/mL at 25 °C (Cold)

Température de stockage

−20°C

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Description générale

Research area: Cell Signaling

Alcohol Oxidase (AOX) is a homo-octamer composed of eight flavin adenine dinucleotide (FAD) cofactors and belongs to the glucose-methanol-choline (GMC) family of oxidoreductases. The AOX1 and AOX2 genes are responsible for encoding AOX. Alcohol oxidase is primarily localized in the peroxisome but is also found in the cytoplasm. Alcohol oxidase is a 600 kDa homooctomeric flavoprotein with eight equal 74 kDa subunits; each containing a flavin adenine dinucleotide (FAD) molecule.

Application

Alcohol oxidase has been used:
  • to catalyze the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes .
  • to study methanol metabolism in yeasts, such as Candida, Pichia, and Hansenula.
  • to study protein translocation into peroxisomes.
  • for the determination of ethanol concentration in alcoholic drinks using enzymatic assay.
  • in development of enzyme electrode for the determination of alcohols.

Actions biochimiques/physiologiques

Alcohol oxidase has the highest affinity for methanol. The affinity decreases with increasing chain length of the alkyl (R) group. The enzyme shows little activity toward secondary, tertiary, or aromatic alcohols; or aliphatic alcohols with a chain length of more than 5 carbons. The pH range for activity of this product is 6.5-8.5, with the optimum pH being 7.5. Alcohol oxidases facilitate the conversion of alcohol into carbonyl compounds while producing hydrogen peroxide. It is also the first enzyme in the yeast methanol utilization pathway.

Définition de l'unité

One unit will oxidize 1.0 μmole of methanol to formaldehyde per min at pH 7.5 at 25 °C.

Forme physique

Contains potassium phosphate buffer salts, DTE, and stabilizer

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)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Alcohol oxidase from Candida boidinii.
H Sahm et al.
Methods in enzymology, 89 Pt D, 424-428 (1982-01-01)
B Vinet
Clinical chemistry, 33(12), 2204-2208 (1987-12-01)
This method for the specific determination of methanol in serum is based on the following two reactions: (formula; see text) Alcohol oxidase is not specific: it converts all lower alcohols to their corresponding aldehydes; however, formaldehyde dehydrogenase is specific and
Yu Sasano et al.
FEMS yeast research, 10(5), 535-544 (2010-05-25)
We identified a gene, designated TRM2, responsible for methanol-inducible gene expression in the methylotrophic yeast Candida boidinii. The encoded protein Trm2p contains two C(2)H(2)-type zinc finger motifs near the N terminus and shows high similarity to Saccharomyces cerevisiae Adr1p and
Ping Zhang et al.
Applied and environmental microbiology, 76(18), 6108-6118 (2010-07-27)
In this work, the identification and characterization of two hexose transporter homologs in the methylotrophic yeast Pichia pastoris, P. pastoris Hxt1 (PpHxt1) and PpHxt2, are described. When expressed in a Saccharomyces cerevisiae hxt-null mutant strain that is unable to take
Yasutaka Sasaki et al.
Journal of bioscience and bioengineering, 110(2), 147-151 (2010-06-16)
We have cloned a gene encoding an alcohol oxidase (AOD) specific to aldehyde alcohols from Paenibacillus sp. AIU 311. The AOD gene contains an open reading frame consisting of 618 nucleotides corresponding to 205 amino acid residues. The deduced amino
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Protocoles

Enzymatic Assay of Alcohol Oxidase (EC 1.1.3.13)

This procedure may be used for all Alcohol Oxidase products. The continuous spectrophotometric rate determination (A405, Light path = 1 cm) is based on the following reactions.

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