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Literature summary for 1.2.3.14 extracted from

  • Zarepour, M.; Simon, K.; Wilch, M.; Nielaender, U.; Koshiba, T.; Seo, M.; Lindel, T.; Bittner, F.
    Identification of superoxide production by Arabidopsis thaliana aldehyde oxidases AAO1 and AAO3 (2012), Plant Mol. Biol., 80, 659-671.
    View publication on PubMed

Cloned(Commentary)

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

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 1–16%, NADH oxidation activity of AAO1 and AAO3 is highly sensitive to DPI treatment Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q7G9P4
-
-

Purification (Commentary)

Purification (Comment) Organism
by affinity chromatography with nickel-nitrilotriacetic acid-agarose under native conditions, further purification by anion exchange chromatography Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
rosette leaf extracts from drought stressed leaves, AAO3 Arabidopsis thaliana
-
seedling AAO1 Arabidopsis thaliana
-

Specific Activity [micromol/min/mg]

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 1–16% 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 and Products (Substrate)

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

Synonyms Comment Organism
AAO1
-
Arabidopsis thaliana
AAO3
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
additional information presence of all prosthetic groups confirmed by UV–vis spectroscopy Arabidopsis thaliana