Cloned (Comment) | Organism |
---|---|
cDNAs of AAO1 and AAO3 expressed in Pichia pastoris to obtain recombinant homodimeric AAO1 and AAO3 proteins with His6-tag | Arabidopsis thaliana |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cyanide | the ability of AAO1 and AAO3 to reduce 2,6-dichloroindophenol is abrogated when the enzymes are pre-treated with cyanide, NADH oxidation activity of AAO1 and AAO3 is highly sensitive to cyanide treatment | Arabidopsis thaliana | |
diphenylene iodonium | DPI i.e. diphenylene iodonium, in the presence of DPI aldehyde oxidation activities of AAO1 and AAO3 are strongly reduced to 116%, NADH oxidation activity of AAO1 and AAO3 is highly sensitive to DPI treatment | Arabidopsis thaliana |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | Q7G9P4 | - |
- |
Purification (Comment) | Organism |
---|---|
by affinity chromatography with nickel-nitrilotriacetic acid-agarose under native conditions, further purification by anion exchange chromatography | Arabidopsis thaliana |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
rosette leaf | extracts from drought stressed leaves, AAO3 | Arabidopsis thaliana | - |
seedling | AAO1 | Arabidopsis thaliana | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
in the presence of diphenylene iodonium, aldehyde oxidation activities of AAO1 and AAO3 are strongly reduced to 116% | Arabidopsis thaliana |
0.093 | - |
heptaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.11 | - |
benzaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.146 | - |
benzaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.204 | - |
indole-3-carbaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.215 | - |
NADH oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.515 | - |
abscisic aldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.517 | - |
heptaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.53 | - |
NADH oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.558 | - |
indole-3-carbaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
0.635 | - |
abscisic aldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication | Arabidopsis thaliana |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
abscisic aldehyde + 2,6-dichloroindophenol | 2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen | Arabidopsis thaliana | abscisic acid + H2O2 | rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2- | ? | |
benzaldehyde + 2,6-dichloroindophenol | 2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen | Arabidopsis thaliana | benzoic acid + H2O2 | rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2- | ? | |
heptaldehyde + 2,6-dichloroindophenol | 2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen | Arabidopsis thaliana | heptanoic acid + H2O2 | rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2- | ? | |
indole-3-carbaldehyde + 2,6-dichloroindophenol | 2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen | Arabidopsis thaliana | indole-3-carboxylate + H2O2 | rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2- | ? | |
additional information | confirmation of superoxide generation by AAO1 and AAO3 by monitoring the reduction of the tetrazolium salt XTT due to O2- | Arabidopsis thaliana | ? | - |
? | |
NADH + O2 | oxidation of NADH by AAO1 and AAO3, no oxidation of NADPH by AAO1 or AAO3 | Arabidopsis thaliana | NAD+ + O2- | for confirmation, O2--dependent reduction of cytochrome c monitored, oxidation of NADH by AAO1 and AAO3 does not result in detectable levels of H2O2 | ? |
Synonyms | Comment | Organism |
---|---|---|
AAO1 | - |
Arabidopsis thaliana |
AAO3 | - |
Arabidopsis thaliana |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | presence of all prosthetic groups confirmed by UVvis spectroscopy | Arabidopsis thaliana |