Indole-3-acetaldehyde oxidase
| indole-3-acetaldehyde oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.3.7 | ||||||||
| CAS no. | 66082-22-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, indole-3-acetaldehyde oxidase (EC 1.2.3.7) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are indole-3-acetaldehyde, water, and oxygen. Its products are indole-3-aceticacid and hydrogen peroxide.[1][2][3][4][5]
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: flavin adenine dinucleotide, heme, and molybdenum.[6][7][8]
References
- ^ Enzyme 1.2.3.7 at KEGG Pathway Database.
- ^ Bower PJ, Brown HM, Purves WK (1978). "Cucumber seedling indoleacetaldehyde oxidase". Plant Physiol. 61 (1): 107–110. doi:10.1104/pp.61.1.107. PMC 1091807. PMID 16660220.
- ^ Miyata S, Suzuki Y, Kamisaka S, Masuda Y (1981). "Indole-3-acetaldehyde oxidase of pea-seedlings". Physiol. Plant. 51 (4): 402–406. Bibcode:1981PPlan..51..402M. 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. Bibcode:1971PPlan..24..272R. doi:10.1111/j.1399-3054.1971.tb03491.x.
- ^ 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.
- ^ 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.