L-aspartat oksidaza
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| L-aspartat oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.4.3.16 | ||||||||
| CAS broj | 69106-47-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
L-aspartat oksidaza (EC 1.4.3.16, NadB, Laspo, AO) je enzim sa sistematskim imenom L-aspartat:kiseonik oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-aspartat + O2 iminozukcinat +H2O2
Ovaj enzim je flavoprotein (FAD). L-aspartatna oksidaza katalizuje prvi korak de novo biosinteza NAD+ kod nekih bakterija.
Reference[uredi | uredi kod]
- ↑ Nasu, S., Wicks, F.D. and Gholson, R.K. (1982). „L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase”. J. Biol. Chem. 257: 626-632. PMID 7033218.
- ↑ Mortarino, M., Negri, A., Tedeschi, G., Simonic, T., Duga, S., Gassen, H.G. and Ronchi, S. (1996). „L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition”. Eur. J. Biochem. 239: 418-426. PMID 8706749.
- ↑ Tedeschi, G., Negri, A., Mortarino, M., Ceciliani, F., Simonic, T., Faotto, L. and Ronchi, S. (1996). „L-Aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity”. Eur. J. Biochem. 239: 427-433. PMID 8706750.
- ↑ Mattevi, A., Tedeschi, G., Bacchella, L., Coda, A., Negri, A. and Ronchi, S. (1999). „Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family”. Structure 7: 745-756. PMID 10425677.
- ↑ Bossi, R.T., Negri, A., Tedeschi, G. and Mattevi, A. (2002). „Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis”. Biochemistry 41: 3018-3024. PMID 11863440.
- ↑ Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. (2006). „Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid”. Plant Physiol. 141: 851-857. PMID 16698895.
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.