Indole-3-acetaldehyde oxidase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is (indol-3-yl)acetaldehyde:oxygen oxidoreductase. Other names in common use include indoleacetaldehyde oxidase, IAAld oxidase, AO1, and indole-3-acetaldehyde:oxygen oxidoreductase. This enzyme participates in tryptophan metabolism. It has 3 cofactors: FAD, Heme, and Molybdenum.

References

Bower PJ, Brown HM, Purves WK (1978). "Cucumber seedling indoleacetaldehyde oxidase". Plant Physiol. 61 (1): 107–110. doi:10.1104/pp.61.1.107.
Miyata S, Suzuki Y, Kamisaka S, Masuda Y (1981). "Indole-3-acetaldehyde oxidase of pea-seedlings". Physiol. Plant. 51 (4): 402–406. doi:10.1111/j.1399-3054.1981.tb05577.x.
Rajagopal R (1971). "Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles". Physiol. Plant. 24 (2): 272–281. doi:10.1111/j.1399-3054.1971.tb03491.x.
Koshiba T, Saito E, Ono N, Yamamoto N, Sato M (1996). "Purification and Properties of Flavin- and Molybdenum-Containing Aldehyde Oxidase from Coleoptiles of Maize". Plant. Physiol. 110 (3): 781–789. doi:10.1104/pp.110.3.781. PMC 157777. PMID 12226218.
Koshiba T, Matsuyama H (1993). "An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts". Plant. Physiol. 102 (4): 1319–1324. doi:10.1104/pp.102.4.1319. PMC 158922. PMID 12231908.
Marion-Poll A, Caboche M, Kamiya Y, Koshiba T (1998). "Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana". Plant. Cell. Physiol. 39 (4): 433–42. doi:10.1093/oxfordjournals.pcp.a029387. PMID 9615466.
T; Akaba, S; Oritani, T; Delarue, M; Bellini, C; Caboche, M; Koshiba, T (1998). "Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana". Plant. Physiol. 116 (2): 687–93. doi:10.1104/pp.116.2.687. PMC 35127. PMID 9489015.

Aldehyde/oxo oxidoreductases (EC 1.2)

1.2.1: NAD or NADP	Aldehyde dehydrogenase Acetaldehyde dehydrogenase Long-chain-aldehyde dehydrogenase

1.2.2: cytochrome	Formate dehydrogenase (cytochrome)

1.2.3: oxygen	Aldehyde oxidase

1.2.4: disulfide	Oxoglutarate dehydrogenase complex Pyruvate dehydrogenase Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD

1.2.7: iron-sulfur protein	Pyruvate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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