Indol-3-acetaldehid oksidaza
| Indol-3-acetaldehid oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.2.3.7 | ||||||||
| CAS broj | 66082-22-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | 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[uredi | uredi kod]
- ↑ 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. and 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[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.