LMPD Database

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LMP010500

UniProt Annotations

Entry Information
Gene Namealdehyde oxidase 2
Protein EntryALDO2_ARATH
UniProt IDQ7G192
SpeciesArabidopsis
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=57 uM for heptaldehyde {ECO:0000269|PubMed:10739959}; KM=7.7 uM for benzaldehyde {ECO:0000269|PubMed:10739959}; KM=0.33 uM for naphthaldehyde {ECO:0000269|PubMed:10739959}; KM=410 uM for cinnamaldehyde {ECO:0000269|PubMed:10739959}; Vmax=24 nmol/min/mg enzyme with heptaldehyde as substrate {ECO:0000269|PubMed:10739959}; Vmax=8.7 nmol/min/mg enzyme with benzaldehyde as substrate {ECO:0000269|PubMed:10739959}; Vmax=65 nmol/min/mg enzyme with naphthaldehyde as substrate {ECO:0000269|PubMed:10739959}; Vmax=20 nmol/min/mg enzyme with cinnamaldehyde as substrate {ECO:0000269|PubMed:10739959}; Note=Kinetic values were obtained with the AO-gamma dimer.; pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:10739959}; Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:10739959};
Catalytic Activity(Indol-3-yl)acetaldehyde + H(2)O + O(2) = (indol-3-yl)acetate + H(2)O(2). {ECO:0000269|PubMed:10423535}.
CofactorName=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CofactorName=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250};
CofactorName=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; Evidence={ECO:0000250}; Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
Enzyme RegulationStrongly inhibited by iodoacetate, potassium cyanide (KCN), 2-mercaptoethanol, dithiothreitol (DTT), p- chloromercuribenzoate, menadione and estradiol. Weakly inhibited by 4'-(9-acridinylamino)methanesulfon-m-anisidine (mAMSA) and tritonX-100. Not affected by allopurinol. {ECO:0000269|PubMed:10739959}.
FunctionIn higher plant aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. In vitro, AO-gamma uses heptaldehyde, benzaldehyde, naphthaldehyde and cinnamaldehyde as substrates; AO-beta uses indole-3-acetaldehyde (IAAld), indole-3- aldehyde (IAld) and naphtaldehyde; the AAO2-AAO3 dimer uses abscisic aldehyde.
SimilarityBelongs to the xanthine dehydrogenase family. {ECO:0000305}.
SimilarityContains 1 2Fe-2S ferredoxin-type domain. {ECO:0000255|PROSITE-ProRule:PRU00465}.
SimilarityContains 1 FAD-binding PCMH-type domain. {ECO:0000255|PROSITE-ProRule:PRU00718}.
Subcellular LocationCytoplasm {ECO:0000305}.
SubunitAldehyde oxidases (AO) are homodimers and heterodimers of AO subunits. AO-beta is a AAO1-AAO2 heterodimer; AO-gamma is a AAO2 homodimer. AAO2 also forms a dimer with AAO3. {ECO:0000269|PubMed:10423535, ECO:0000269|PubMed:15064376}.
Tissue SpecificityWeakly expressed in roots, leaves and seedlings. In seedlings, mostly expressed in lower part of hypocotyls. Detectable in seeds and mature siliques at low levels. {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:9489015, ECO:0000269|PubMed:9615466, ECO:0000269|PubMed:9655945}.