1.1.3.13: alcohol oxidase
This is an abbreviated version!
For detailed information about alcohol oxidase, go to the full flat file.
Word Map on EC 1.1.3.13
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1.1.3.13
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pichia
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pastoris
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methylotrophic
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polymorpha
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hansenula
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biosensors
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catalase
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formaldehyde
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electrode
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candida
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methanol-inducible
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oxidases
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amperometric
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boidinii
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alpha-factor
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analysis
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methanol-utilizing
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flavoenzyme
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octameric
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dihydroxyacetone
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methanolica
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methanol-grown
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vanillyl
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microbodies
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alpha-mating
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isoamyl
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coniferyl
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ogataea
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komagataella
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ppic9k
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biotechnology
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peroxisome-deficient
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synthesis
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molecular biology
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degradation
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simplicissimum
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zeocin
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screen-printed
- 1.1.3.13
- pichia
- pastoris
-
methylotrophic
- polymorpha
- hansenula
-
biosensors
- catalase
- formaldehyde
-
electrode
- candida
-
methanol-inducible
- oxidases
-
amperometric
- boidinii
- alpha-factor
- analysis
-
methanol-utilizing
-
flavoenzyme
-
octameric
- dihydroxyacetone
- methanolica
-
methanol-grown
-
vanillyl
- microbodies
-
alpha-mating
-
isoamyl
-
coniferyl
-
ogataea
- komagataella
-
ppic9k
- biotechnology
-
peroxisome-deficient
- synthesis
- molecular biology
- degradation
- simplicissimum
-
zeocin
-
screen-printed
Reaction
Synonyms
alcohol oxidase 1, alcohol oxidase 2, alcohol oxidase A, alcohol oxidase B, alcohol oxidase I, alcohol: O2 oxidoreductase, alcohol:dioxygen-oxidoreductase, alcohol:O2 oxidoreductase, AlcOx, AOd, AOD1, AOext, AOint, AOX, AOX1, AOX2, AOXI, broad substrate specific alcohol oxidase, EC 1.1.3.31, ethanol oxidase, extracellular alcohol oxidase, FAD-dependent alcohol oxidase, FAO1, GLRG_05590, intracellular alcohol oxidase, long chain fatty alcohol oxidase, methanol oxidase, Mod1p, Mod2p, oxidase, alcohol, P-AOD, peroxisomal alcohol oxidase, primary alcohol oxidase, SCAO, short chain alcohol oxidase, short-chain alcohol oxidase, VAO, veratryl alcohol oxidase
ECTree
1.1.3.13 alcohol oxidaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.3.13 - alcohol oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
M359R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
S101A
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
S101A/D250G/F253R/V355T/F357R/M359R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13, with a 20fold increased kcat compared to that of the wildtype enzyme. This variant enables the oxidation of 10 mM hexanol to hexanal in less than 24h with 100% conversion and catalyzes significantly improved oxidation of saturated, unsaturated, aliphatic, cyclic and benzylic alcohols
S101A/V355T/F357R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
S101A/V355T/F357R/M359R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
V355T/F357R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
G15A
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mutastion in putative FAD-binding domain, prevents enzyme import into peroxisome and assembly
F101N
with enlarged catalytic cavity, increase in activity with substrates 1-propanol, glycerol, (R)-1,2-propanediol
F101S
with enlarged catalytic cavity, retains a high degree of thermostability
M103S
with enlarged catalytic cavity, increase in activity with substrates 1-propanol, glycerol, (R)-1,2-propanediol
additional information
additional information
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construction of an inactive double-knockout mutant of FAO1 by gene deletion, the mutant is incapable to grow on octadecane, but grows well on oleic acid, palmitic acid, and shorter chain alkanes/fatty acids, overview, an additional spontenaous mutation of the double mutant leads to loss of the ability to grow on oleic acid and hexadecane
additional information
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analysis of the regulation of native alcohol oxidase expression in Pichia pastoris Mut+ strain expressing a recombinant avidin
additional information
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the alcohol oxidase is immobilized on nanoporous aluminium oxide membranes by silanization and activation by carbonyldiimidazole to create a flow-through enzyme reactor, method optimization, overview. The immobilized alcohol oxidase shows high productivity in hydrogen peroxide generation from methanol, and retains about 58% of initial activity after 3 weeks of storage and repeated use with pH 6.5 and at room temperature. Construction of a bienzymatic modular reactor with horseradish peroxidase and alcohol oxidase, overview
additional information
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alcohol dehydrogenase is expressed with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D) and purified. The resulting bifunctional biocatalyst retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidase, while merely requiring a catalytic amount of NADP+
additional information
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deletion of 1,4,10, or 16 C-terminal amino acids, normal import into peroxisome and assembly to octamer. Deletion of C-terminal 22 amino acids, growth of cells ceases at an OD corresponding to midexponential growth stage, more than 90% reduction of enzymic activity, enzyme is localized both to peroxisome and cytosol
additional information
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isoation of mutant strain by UV treatment, with constitutive alcohol oxidase and peroxisome biosynthesis, mutant enzyme activity is about 2fold that of wild type
additional information
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in mutants defective in matrix protein import, cytosolic enzyme crystalloids are formed, mutants that contain enzymatically active enzyme in the cytosol are impaired in growth on methanol as a sole source of carbon and energy
additional information
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enzyme immobilization on DEAE-cellulose particles for alcohol biosensor applications, substrate specificity and the optimum pH of the immobilized enzyme are similar to those of the free enzyme, while Km and temperature optimum differ, overview
additional information
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strain lacking isoform Mod1, severe growth inhibition on 0.1% methanol, growth is restored with increase in methanol concentration
additional information
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two mutant strains possess defects in genes MTH1 and MTH2, which result in the inability to assimilate methanol as a sole carbon source and increased activity of alcohol oxidase, AO. The mutant mth1 possesses a dominant formation of AO isoform with electrophoretic mobility which is typical for isogenic form 9, the product of the AUG2 gene, and a decreased level of peroxisomal catalase, phenotypes, overview
additional information
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alcohol dehydrogenase is expressed with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D) and purified. The resulting bifunctional biocatalyst retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidase, while merely requiring a catalytic amount of NADP+
