3-izopropilmalat dehidrogenaza
(Preusmjereno sa stranice EC 1.1.1.85)
3-izopropilmalat dehidrogenaza (EC 1.1.1.85, beta-isopropilmalatni enzim, beta-izopropilmalatna dehidrogenaza, treo-Ds-3-izopropilmalatna dehidrogenaza, 3-karboksi-2-hidroksi-4-metilpentanoat:NAD+ oksidoreduktaza) je enzim sa sistematskim imenom (2R,3S)-3-izopropilmalat:NAD+ oksidoreduktaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 3-izopropilmalat dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.1.1.85 | ||||||||
| CAS broj | 9030-97-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (2R,3S)-3-izopropilmalat + NAD+ 4-metil-2-oksopentanoat + CO2 + NADH + H+ (sveukupna reakcija)
- (1a) (2R,3S)-3-izopropilmalat + NAD+ (2S)-2-izopropil-3-oksosukcinat + NADH + H+
- (1b) (2S)-2-izopropil-3-oksosukcinat 4-metil-2-oksopentanoat + CO2 (spontano)
Produkt se spontano dekarboksiluje i proizvodi 4-metil-2-oksopentanoat.
Reference uredi
- ↑ Burns, R.O., Umbarger, H.E. and Gross, S.R. (1963). „The biosynthesis of leucine. III. The conversion of α-hydroxy-β-carboxyisocaproate to α-ketoisocaproate”. Biochemistry 2: 1053-1053. PMID 14087358.
- ↑ Parsons, S.J. and Burns, R.O. (1969). „Purification and properties of β-isopropylmalate dehydrogenase”. J. Biol. Chem. 244: 996-1003. PMID 4889950.
- ↑ Németh, A., Svingor, Á., Pócsik, M., Dobó, J., Magyar, C, Szilaaagyi, A., Gál, P. and Závodszky, P. (2000). „Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase”. FEBS Lett. 468: 48-52. PMID 10683439.
- ↑ Calvo, J. (1964). „M., Stevens, C. M., Kalyanpur, M. G., and Umbarger, H. E. The absolute configuration of α-hydroxy-β-carboxyisocaproic acid (3-isopropylmalic acid), an intermediate in leucine biosynthesis”. Biochemistry 3: 2024-2027. PMID 14269331.
Literatura uredi
- 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.