LMPD Database

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LMP010501

UniProt Annotations

Entry Information
Gene Namealdehyde oxidase 1
Protein EntryALDO1_ARATH
UniProt IDQ7G193
SpeciesArabidopsis
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=14 uM for heptaldehyde {ECO:0000269|PubMed:10739959}; KM=19 uM for protocatechualdehyde {ECO:0000269|PubMed:10739959}; KM=0.74 uM for benzaldehyde {ECO:0000269|PubMed:10739959}; KM=4.4 uM for indole-3-aldehyde {ECO:0000269|PubMed:10739959}; KM=39 uM for indole-3-acetaldehyde {ECO:0000269|PubMed:10739959}; KM=20 uM for cinnamaldehyde {ECO:0000269|PubMed:10739959}; KM=22 uM for citral {ECO:0000269|PubMed:10739959}; Vmax=7.1 nmol/min/mg enzyme with heptaldehyde as substrate {ECO:0000269|PubMed:10739959}; Vmax=8.0 nmol/min/mg enzyme with protocatechualdehyde as substrate {ECO:0000269|PubMed:10739959}; Vmax=17 nmol/min/mg enzyme with benzaldehyde as substrate {ECO:0000269|PubMed:10739959}; Vmax=6.9 nmol/min/mg enzyme with IAld as substrate {ECO:0000269|PubMed:10739959}; Vmax=7.3 nmol/min/mg enzyme with IAAld as substrate {ECO:0000269|PubMed:10739959}; Vmax=3.8 nmol/min/mg enzyme with cinnamaldehyde as substrate {ECO:0000269|PubMed:10739959}; Vmax=38 nmol/min/mg enzyme with citral as substrate {ECO:0000269|PubMed:10739959}; Note=Kinetic values were obtained with the AO-alpha dimer.; pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:10739959}; Temperature dependence: Optimum temperature is 65 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, ECO:0000269|PubMed:10739959, ECO:0000269|PubMed:9489015}.
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 and potassium cyanide (KCN). Weakly inhibited by 2-mercaptoethanol, dithiothreitol (DTT), menadione, estradiol, 4'-(9- acridinylamino)methanesulfon-m-anisidine (mAMSA), allopurinol and tritonX-100. Not affected by p-chloromercuribenzoate. {ECO:0000269|PubMed:10739959}.
FunctionIn higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. AO-alpha may be involved in the biosynthesis of auxin, and in biosynthesis of abscisic acid (ABA) in seeds. In vitro, AO-alpha uses heptaldehyde, protocatechualdehyde, benzaldehyde, indole-3-aldehyde (IAld), indole-3-acetaldehyde (IAAld), cinnamaldehyde and citral as substrates; AO-beta uses IAAld, IAld and naphtaldehyde as substrates. {ECO:0000269|PubMed:9489015}.
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-alpha is an AAO1 homodimer; AO-beta is an AAO1- AAO2 heterodimer. {ECO:0000269|PubMed:10423535}.
Tissue SpecificityPredominantly expressed in roots, seedlings, mature siliques and seeds, and to lower extent in stems and rosettes. In seedlings, mostly expressed in lower part of hypocotyls and roots. {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:9489015, ECO:0000269|PubMed:9615466, ECO:0000269|PubMed:9655945}.