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Information on EC 1.1.3.13 - alcohol oxidase and Organism(s) Pichia angusta and UniProt Accession P04841

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.13 alcohol oxidase
IUBMB Comments
The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor [1,3]. The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism . The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols.
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This record set is specific for:
Pichia angusta
UNIPROT: P04841
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alcohol oxidase, alcohol oxidase 1, methanol oxidase, alcohol oxidase i, ethanol oxidase, peroxisomal alcohol oxidase, mod1p, mod2p, alcohol oxidase a, alcox, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ethanol oxidase
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oxidase, alcohol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
alcohol:oxygen oxidoreductase
The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor [1,3]. The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism [4]. The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols.
CAS REGISTRY NUMBER
COMMENTARY hide
9073-63-6
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALOX_PICAN
664
0
74089
Swiss-Prot
other Location (Reliability: 2)