Piruvat sintaza
| Piruvat sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.2.7.1 | ||||||||
| CAS broj | 9082-51-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Piruvat sintaza (EC 1.2.7.1, piruvatna oksidoreduktaza, piruvatna sintetaza, piruvat:feredoksin oksidoreduktaza, piruvinska-feredoksinska oksidoreduktaza) je enzim sa sistematskim imenom piruvat:feredoksin 2-oksidoreduktaza (KoA-acetilacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- piruvat + KoA + 2 oksidovani feredoksin acetil-KoA + CO2 + 2 redukovani feredoksin + 2 H+
Ovaj enzim sadrži tiamin difosfat i [4Fe-4S] klastere. On je jedan od četiri 2-oksokiselinske oksidoreduktaze koji se razlikujuj po njihovoj sposobnosti da oksidativno dekarboksiluju različite 2-oksokiseline i formiraju KoA derivate, cf. EC 1.2.7.3, 2-oksoglutarat sintaza, EC 1.2.7.7, 3-metil-2-oksobutanoat dehidrogenaza (feredoksin) i EC 1.2.7.8, indolpiruvat feredoksin oksidoreduktaza.
Reference
- ↑ Evans, M.C.W. and Buchanan, B.B. (1965). „Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium”. Proc. Natl. Acad. Sci. USA 53: 1420-1425. PMID 5217644.
- ↑ Gehring, U. and Arnon, D.I. (1972). „Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium”. J. Biol. Chem. 247: 6963-6969. PMID 4628267.
- ↑ Uyeda, K. and Rabinowitz, J.C. (1971). „Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme”. J. Biol. Chem. 246: 3111-3119. PMID 5574389.
- ↑ Uyeda, K. and Rabinowitz, J.C. (1971). „Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism”. J. Biol. Chem. 246: 3120-3125. PMID 4324891.
- ↑ Charon, M.-H., Volbeda, A., Chabriere, E., Pieulle, L. and Fontecilla-Camps, J.C. (1999). „Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase”. Curr. Opin. Struct. Biol. 9: 663-669. PMID 10607667.
Literatura
- 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.
Spoljašnje veze
- MeSH Pyruvate+synthase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
