Glutaril-KoA dehidrogenaza
| Glutaril-KoA dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Glutaril-KoA dehidrogenaza tetramer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.3.8.6 | ||||||||
| CAS broj | 37255-38-2 | ||||||||
| 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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Glutaril-KoA dehidrogenaza (EC 1.3.8.6, glutarilna koenzim A dehidrogenaza, glutaril-KoA:(akceptor) 2,3-oksidoreduktaza (dekarboksilacija)) je enzim sa sistematskim imenom glutaril-KoA:elektron-transfer flavoprotein 2,3-oksidoreduktaza (dekarboksilacija).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- glutaril-KoA + elektron-transfer flavoprotein (E)-but-2-enoil-KoA + CO2 + redukovani elektron-transfer flavoprotein (sveukupna reakcija)
- (1a) glutaril-KoA + elektron-transfer flavoprotein (2E)-4-karboksibut-2-enoil-KoA + redukovani elektron-transfer flavoprotein
- (1b) (2E)-4-karboksibut-2-enoil-KoA (E)-but-2-enoil-KoA + CO2
Ovaj enzim sadrži FAD. Enzim katalizuje oksidaciju glutaril-KoA do glutakonil-KoA.
Reference
- ↑ Besrat, A., Polan, C.E. and Henderson, L.M. (1969). „Mammalian metabolism of glutaric acid”. J. Biol. Chem. 244: 1461-1467. PMID 4304226.
- ↑ Hartel, U., Eckel, E., Koch, J., Fuchs, G., Linder, D. and Buckel, W. (1993). „Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate”. Arch. Microbiol. 159: 174-181. PMID 8439237.
- ↑ Dwyer, T.M., Zhang, L., Muller, M., Marrugo, F. and Frerman, F. (1999). „The functions of the flavin contact residues, αArg249 and βTyr16, in human electron transfer flavoprotein”. Biochim. Biophys. Acta 1433: 139-152. PMID 10446367.
- ↑ Rao, K.S., Albro, M., Dwyer, T.M. and Frerman, F.E. (2006). „Kinetic mechanism of glutaryl-CoA dehydrogenase”. Biochemistry 45: 15853-15861. PMID 17176108.
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 Glutaryl-CoA+dehydrogenase
- 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
