Izocitrat dehidrogenaza (NADP+)
| Izocitrat dehidrogenaza (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 1.1.1.42 | ||||||||
| CAS broj | 9028-48-2 | ||||||||
| 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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Izocitrat dehidrogenaza (NADP+) (EC 1.1.1.42, oksalosukcinatna dekarboksilaza, oksalsukcinska dekarboksilaza, izocitratna (NADP) dehidrogenaza, izocitratna (nikotinamid adenin dinukleotid fosfat) dehidrogenaza, NADP-specifična izocitratna dehidrogenaza, NADP-vezana izocitratna dehidrogenaza, NADP-zavisna izocitratna dehidrogenaza, NADP isocitratna dehidrogenaza, izocitratna dehidrogenaza (NADP zavisna), NADP-zavisna isocitratna dehidrogenaza, trifosfopiridin nukleotid vezana izocitratna dehidrogenaza - oksalosukcinatna karboksilaza, NADP+-vezana izocitratna dehidrogenaza, NADP+-ICDH, NADP+-IDH, IDP, IDP1, IDP2, IDP3) je enzim sa sistematskim imenom izocitrat:NADP+ oksidoreduktaza (dekarboksilacija).[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- izocitrat + NADP+ 2-oksoglutarat + CO2 + NADPH + H+ (overall reakcija)
- (1a) izocitrat + NADP+ oksalosukcinat + NADPH + H+
- (1b) oksalosukcinat 2-oksoglutarat + CO2
Za aktivaciju su neophodni Mn2+ ili Mg2+. Za razliku od EC 1.1.1.41, izocitratne dehidrogenaze (NAD+), ovaj enzim može da koristiti oksalosukcinat kao supstrat. Kod eukariota, izocitrat dehidrogenaza postoji u dve forme: enzim vezan za NAD+ koji je prisutan samo u mitohondrijama i ispoljava alosterna svojstva, i nealosterni, NADP+-vezani enzim koji je prisutan u mitohondrijama i u citoplazmi. Enzimi pojedinih vrsta takođe mogu da koriste NAD+, ali funkcionišu znatno sporije.
Reference
- ↑ Agosin, M.U. and Weinbach, E.C. (1956). „Partial purification and characterization of the isocitric dehydrogenase from Trypanosoma cruzi”. Biochim. Biophys. Acta 21: 117-126. PMID 13363868.
- ↑ Moyle, J. and Dixon, M. (1956). „Purification of the isocitrate enzyme (triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase)”. Biochem. J. 63: 548-552. PMID 13355848.
- ↑ Plaut, G.W.E. (1963). „Isocitrate dehydrogenases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 105-126.
- ↑ Siebert, G., Dubuc, J., Warner, R.C. and Plaut, G.W.E. (1957). „The preparation of isocitrate dehydrogenase from mammalian heart”. J. Biol. Chem. 226: 965-975. PMID 13438885.
- ↑ Vickery, H.B. (1962). „A suggested new nomenclature for the isomers of isocitric acid”. J. Biol. Chem. 237: 1739-1741. PMID 13925783.
- ↑ Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and Hough, D.W. (1995). „Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence”. FEMS Microbiol. Lett. 134: 85-90. PMID 8593959.
- ↑ Steen, I.H., Lien, T. and Birkeland, N.-K. (1997). „Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus”. Arch. Microbiol. 168: 412-420. PMID 9325430.
- ↑ Koh, H.J., Lee, S.M., Son, B.G., Lee, S.H., Ryoo, Z.Y., Chang, K.T., Park, J.W., Park, D.C., Song, B.J., Veech, R.L., Song, H. and Huh, T.L. (2004). „Cytosolic NADP+-dependent isocitrate dehydrogenase plays a key role in lipid metabolism”. J. Biol. Chem. 279: 39968-39974. PMID 15254034.
- ↑ Ceccarelli, C., Grodsky, N.B., Ariyaratne, N., Colman, R.F. and Bahnson, B.J. (2002). „Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism”. J. Biol. Chem. 277: 43454-43462. PMID 12207025.
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.