Glutamat sintaza (feredoksin)
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Glutamat sintaza (feredoksin) | |||||||||
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Identifikatori | |||||||||
EC broj | 1.4.7.1 | ||||||||
CAS broj | 62213-56-3 | ||||||||
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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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[uredi | uredi kod]
- ↑ 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. and 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[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.