Synonym: Alcohol:oxygen oxidoreductase
|Related Categories||1.1.x.x Acting on hydroxyl groups, 1.x.x.x Oxidoreductases, Alcohol Metabolism, Application Index, Biochemicals and Reagents,|
|form||buffered aqueous solution|
|shipped in||dry ice|
One unit will oxidize 1.0 μmole of methanol to formaldehyde per min at pH 7.5 at 25 °C.
Solution in 30% sucrose with 0.1 M phosphate buffer at pH 8.0
Alcohol Oxidase may be used to study protein translocation into peroxisomes. Product A2404 is from Pichia pastoris. It has been used for the bacterial expression and immunological verification of Hv-p68 cDNA clones 1.
Alcohol oxidase catalyzes the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes. It has the highest affinity for methanol. Alcohol oxidase is involved in the metabolism of methanol, which is important for yeasts that utilize methanol as their sole energy source. Alcohol oxidase is primarily found in the peroxisome but may be present in the cytoplasm as well.
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lyophilized powder, 5-15 units/mg protein
vacuum-dried powder, ≥0.6 units/mg solid
lyophilized powder, 1.0-6.0 units/mg solid
Type VI-A, essentially salt-free, lyophilized powder, 950-2000 units/mg solid (using ABTS), 250-330 units/mg solid (using pyrogallol)
The continuous spectrophotometric rate determination (A405, Light path = 1 cm) is based on the following reactions:
Keywords: Enzyme activity, Extinction coefficient
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Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
1. A novel alcohol oxidase/RNA-binding protein with affinity for mycovirus double-stranded RNA from the filamentous fungus Helminthosporium (Cochliobolus) victoriae: molecular and functional characterization. Ana I. Soldevila, et al. J. Biol. Chem. 276, 4652-4661, (2001)
Trm2p-dependent derepression is essential for methanol-specific gene activation in the methylotrophic yeast Candida boidinii. Sasano Y, Yurimoto H, Kuriyama M, et al. FEMS Yeast Res. 10(5), 535-44, (2010)
Biosynthetic pathways of the sex pheromone components and substrate selectivity of the oxidation enzymes working in pheromone glands of the fall webworm, Hyphantria cunea. Kiyota R, Arakawa M, Yamakawa R, et al. Insect Biochem. Mol. Biol. 41(6), 362-9, (2011)
High-throughput screening and characterization of xylose-utilizing, ethanol-tolerant thermophilic bacteria for bioethanol production. Qi X, Zhang Y, Tu R, et al. J. Appl. Microbiol. 110(6), 1584-91, (2011)
Improvement of porcine interferon-α production by recombinant Pichia pastoris via induction at low methanol concentration and low temperature. Jin H, Liu G, Dai K, et al. Appl. Biochem. Biotechnol. 165(2), 559-71, (2011)
Analysis of the 5' untranslated region (5'UTR) of the alcohol oxidase 1 (AOX1) gene in recombinant protein expression in Pichia pastoris. Staley CA, Huang A, Nattestad M, et al. Gene 496(2), 118-27, (2012)
Determination of trace copper ions with ultrahigh sensitivity and selectivity utilizing CdTe quantum dots coupled with enzyme inhibition. Guo C, Wang J, Cheng J, et al. Biosens. Bioelectron. 36(1), 69-74, (2012)
Heterologous protein expression in Pichia thermomethanolica BCC16875, a thermotolerant methylotrophic yeast and characterization of N-linked glycosylation in secreted protein. Tanapongpipat S, Promdonkoy P, Watanabe T, et al. FEMS Microbiol. Lett. 334(2), 127-34, (2012)
The zinc finger proteins Mxr1p and repressor of phosphoenolpyruvate carboxykinase (ROP) have the same DNA binding specificity but regulate methanol metabolism antagonistically in Pichia pastoris. Kumar NV and Rangarajan PN J. Biol. Chem. 287(41), 34465-73, (2012)
Alcohol oxidase, a flavoprotein from several Basidiomycetes species. Crystallization by fractional precipitation with polyethylene glycol. Janssen FW and Ruelius HW Biochim. Biophys. Acta 151(2), 330-42, (1968)
Steady-state generation of hydrogen peroxide: kinetics and stability of alcohol oxidase immobilized on nanoporous alumina. Kjellander M, Götz K, Liljeruhm J, et al. Biotechnol. Lett. 35(4), 585-90, (2013)
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