Индол-3-ацеталдехид оксидаза
| Indol-3-acetaldehid oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.2.3.7 | ||||||||
| CAS broj | 66082-22-2 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Indol-3-acetaldehid oksidaza (EC 1.2.3.7, indolacetaldehidna oksidaza, IAAld oksidaza, AO1, indol-3-acetaldehid:kiseonik oksidoreduktaza) je enzim sa sistematskim imenom (indol-3-il)acetaldehid:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (indol-3-il)acetaldehid +H2O + O2 (indol-3-il)acetat +H2O2
Ovaj enzim je hemoprotein. On je izoforma aldehid oksidaze (EC 1.2.3.1). On ima preferenciju za aldehide sa indolnim prstenom. Smatra se da on učestvuje u biosintezi biljnih hormona, jer je njegova aktivnost veća kod mutanata koji prekomerno formiraju auksin, u odnosu na divlji tip Arabidopsis thaliana. Dok je (indol-3-il)acetaldehid preferentni supstrat, ovaj enzim takođe oksiduje indol-3-karbaldehid i acetaldehid, mada sporo. Enzim iz kukuruza sadrži FAD, gvožđe i molibden.
Reference
[уреди | уреди извор]- ^ Bower, P.J., Brown, H.M. and Purves, W.K. (1978). „Cucumber seedling indoleacetaldehyde oxidase”. Plant Physiol. 61: 107—110. PMID 16660220.
- ^ Miyata, S., Suzuki, Y., Kamisaka, S. and Masuda, Y. (1981). „Indole-3-acetaldehyde oxidase of pea-seedlings”. Physiol. Plant. 51: 402—406.
- ^ Rajagopal, R. (1971). „Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles”. Physiol. Plant. 24: 272—281.
- ^ Koshiba, T., Saito, E., Ono, N., Yamamoto, N. and Sato, M. (1996). „Purification and properties of flavin- and molybdenum-containing aldehyde oxidase from coleoptiles of maize”. Plant Physiol. 110: 781—789. 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: 1319—1324. PMID 12231908.
- ^ Sekimoto, H., Seo, M., Kawakami, N., Komano, T., Desloire, S., Liotenberg, S., Marion-Poll, A., Caboche, M., Kamiya, Y. and Koshiba, T. (1998). „Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana”. Plant Cell Physiol. 39: 433—442. PMID 9615466.
- ^ Seo, M., Akaba, S., Oritani, T., Delarue, M., Bellini, C., Caboche, M. and Koshiba, T. (1998). „Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana”. Plant Physiol. 116: 687—693. PMID 9489015.
Literatura
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- Indole-3-acetaldehyde+oxidase на US National Library of Medicine Medical Subject Headings (MeSH)
