Malat dehidrogenaza (oksaloacetat-dekarboksilacija, NADP+)
| Malat dehidrogenaza (oksaloacetat-dekarboksilacija, NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.1.1.40 | ||||||||
| CAS broj | 9028-47-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Malat dehidrogenaza (oksaloacetat-dekarboksilacija, NADP+) (EC 1.1.1.40, malat dehidrogenaza (dekarboksilacija, NADP+), NADP+-vezani dekarboksilacioni malatni enzim, NADP+-malatni enzim, NADP+-specifični malatni enzim, NADP+-specifična malatna dehidrogenaza, malat dehidrogenaza (NADP+, dekarboksilacija), L-malat:NADP+ oksidoreduktaza) je enzim sa sistematskim imenom (S)-malat:NADP+ oksidoreduktaza (oksaloacetatna dekarboksilacija).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (S)-malat + NADP+ piruvat + CO2 + NADPH
- oksaloacetat piruvat + CO2
Ovaj enzim katalizuje oksidativnu dekarboksilaciju (S)-malata u prisustvu NADP+ i divalentnih metalnih jona, i dekarboksilaciju oksaloacetata, cf. EC 1.1.1.38, malatna dehidrogenaza (oksaloacetatna dekarboksilacija), i EC 1.1.1.39, malatna dehidrogenaza (dekarboksilacija).
Reference
- ↑ Harary, I., Korey, S.R. and Ochoa, S. (1953). „B'iosynthesis of dicarboxylic acids by carbon dioxide fixation. VII. Equilibrium of "malic" enzyme reaction”. J. Biol. Chem. 203: 595-604. PMID 13084629.
- ↑ Ochoa, S., Mehler, A.H. and Kornberg, A. (1948). „Biosynthesis of dicarboxylic acids by carbon dioxide fixation. I. Isolation and properties of an enzyme from pigeon liver catalyzing the reversible oxidative decarboxylation of l-malic acid”. J. Biol. Chem. 174: 979-1000. PMID 18871257.
- ↑ Rutter, W.J. and Lardy, H.A. (1958). „Purification and properties of pigeon liver malic enzyme”. J. Biol. Chem. 233: 374-382. PMID 13563505.
- ↑ Stickland, R.G. (1959). „Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate”. Biochem. J. 73: 646-654. PMID 13834656.
- ↑ Stickland, R.G. (1959). „Some properties of the malic enzyme of pigeon liver. 2. Synthesis of malate from pyruvate”. Biochem. J. 73: 654-659. PMID 13834657.
- ↑ Walker, D.A. (1960). „Physiological studies on acid metabolism. 7. Malic enzyme from Kalanchoë crenata: effects of carbon dioxide concentration.”. Biochem. J. 74: 216-223. PMID 13842495.
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.