4-hidroksibenzoil-KoA reduktaza
| 4-hidroksibenzoil-KoA reduktaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.3.7.9 | ||||||||
| CAS broj | 133758-58-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
4-hidroksibenzoil-KoA reduktaza (EC 1.3.7.9, 4-hidroksibenzoil-KoA reduktaza (dehidroksilating), 4-hidroksibenzoil-KoA:(akceptor) oksidoreduktaza) je enzim sa sistematskim imenom benzoil-KoA:akceptor oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- benzoil-KoA + oksidovani feredoksin + H2O 4-hidroksibenzoil-KoA + redukovani feredoksin
Ovaj molibden-flavin-gvožđe-sumpor protein učestvuje u anaerobnom putu fenolnog metabolizma kod bakterija. Feredoksin sa dva [4Fe-4S] klustera funkcioniše kao prirodni donor elektrona.
Reference
- ↑ Glockler, R., Tschech, A. and Fuchs, G. (1989). „Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in a denitrifying, phenol-degrading Pseudomonas species”. FEBS Lett. 251: 237-240. PMID 2753161.
- ↑ Heider, J., Boll, M., Breese, K., Breinig, S., Ebenau-Jehle, C., Feil, U., Gad'on, N., Laempe, D., Leuthner, B., Mohamed, M.E.S., Schneider, S., Burchhardt, G. and Fuchs, G. (1998). „Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica”. Arch. Microbiol. 170: 120-131. PMID 9683649.
- ↑ Breese, K. and Fuchs, G. (1998). „4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica - prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins”. Eur. J. Biochem. 251: 916-923. PMID 9490068.
- ↑ Brackmann, R. and Fuchs, G. (1993). „Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species”. Eur. J. Biochem. 213: 563-571. PMID 8477729.
- ↑ Heider, J. and Fuchs, G. (1997). „Anaerobic metabolism of aromatic compounds”. Eur. J. Biochem. 243: 577-596. PMID 9057820.
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 4-hydroxybenzoyl-CoA+reductase
- 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
