Glutamat sintaza (feredoksin)
| Glutamat sintaza (feredoksin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.4.7.1 | ||||||||
| CAS broj | 62213-56-3 | ||||||||
| 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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Glutamat sintaza (feredoksin) (EC 1.4.7.1, feredoksin-zavisna glutamatna sintaza, feredoksin-glutamatna sintaza, glutamatna sintaza (feredoksin-zavisna)) je enzim sa sistematskim imenom L-glutamat:feredoksin oksidoreduktaza (transaminacija).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2 L-glutamat + 2 oksidovani feredoksin L-glutamin + 2-oksoglutarat + 2 redukovani feredoksin + 2 H+ (sveukupna reakcija)
- (1a) L-glutamat + NH3 L-glutamin +H2O
- (1b) L-glutamat + 2 oksidovani feredoksin +H2O NH3 + 2-oksoglutarat + 2 redukovani feredoksin + 2 H+
Ovaj enzim vezuje 3Fe-4S klaster, FAD i FMN. Protein se sastoji od dva domena, jedan hidrolizuje L-glutamin do NH3 i L-glutamata (cf. EC 3.5.1.2, glutaminaza), a drugi kombinuje proizvedeni NH3 sa 2-oksoglutaratom i formira drugi molekul L-glutamata.
Reference
[уреди | уреди извор]- ^ Galván, F., Márquez, A.J. and Vega, J.M. (1984). „Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardii”. Planta. 162: 180—187.
- ^ Lea, P.J. & Miflin, B.J. (1974). „Alternative route for nitrogen assimilation in higher plants”. Nature (Lond.). 251: 614—616. PMID 4423889.
- ^ Ravasio, S., Dossena, L., Martin-Figueroa, E., Florencio, F.J., Mattevi, A., Morandi, P., Curti, B. and Vanoni, M.A. (2002). „Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated α subunit”. Biochemistry. 41: 8120—8133. PMID 12069605.
- ^ Navarro, F., Martin-Figueroa, E., Candau, P. and Florencio, F.J. (2000). „Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the cyanobacterium Synechocystis sp. PCC 6803: expression and assembly in Escherichia coli”. Arch. Biochem. Biophys. 379: 267—276. PMID 10898944.
- ^ van den Heuvel, R.H., Ferrari, D., Bossi, R.T., Ravasio, S., Curti, B., Vanoni, M.A., Florencio, F.J. and Mattevi, A. (2002). „Structural studies on the synchronization of catalytic centers in glutamate synthase”. J. Biol. Chem. 277: 24579—24583. PMID 11967268.
- ^ van den Heuvel, R.H., Svergun, D.I., Petoukhov, M.V., Coda, A., Curti, B., Ravasio, S., Vanoni, M.A. and Mattevi, A. (2003). „The active conformation of glutamate synthase and its binding to ferredoxin”. J. Mol. Biol. 330: 113—128. PMID 12818206.
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]- Glutamate+synthase+(ferredoxin) на US National Library of Medicine Medical Subject Headings (MeSH)
