L-aspartat oksidaza
| L-aspartat oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.4.3.16 | ||||||||
| CAS broj | 69106-47-4 | ||||||||
| 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 | ||||||||
| |||||||||
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[уреди | уреди извор]
- ^ 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[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.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze[уреди | уреди извор]
- L-aspartate+oxidase на US National Library of Medicine Medical Subject Headings (MeSH)
