Arsenat reduktaza (glutaredoksin)
Arsenat reduktaza (glutaredoksin) (EC 1.20.4.1, Arsenate reductase (glutaredoxin)) je enzim sa sistematskim imenom glutaredoksin:arsenat oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Arsenat reduktaza (glutaredoksin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.20.4.1 | ||||||||
| CAS broj | 146907-46-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- arsenat + glutaredoksin arsenit + glutaredoksin disulfid + H2O
Ovaj enzim je molibdoenzim.
Reference uredi
- ↑ Gladysheva, T., Liu, J.Y. and Rosen, B.P. (1996). „His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773”. J. Biol. Chem. 271: 33256-33260. PMID 8969183.
- ↑ Gladysheva, T.B., Oden, K.L. and Rosen, B.P. (1994). „Properties of the arsenate reductase of plasmid R773”. Biochemistry 33: 7288-7293. PMID 8003492.
- ↑ Holmgren, A. and Aslund, F. (1995). „Glutaredoxin”. Methods Enzymol. 252: 283-292. PMID 7476363.
- ↑ Ji, G.Y., Garber, E.A.E., Armes, L.G., Chen, C.M., Fuchs, J.A. and Silver, S. (1994). „Arsenate reductase of Staphylococcus aureus' plasmid PI258”. Biochemistry 33: 7294-7299.
- ↑ Krafft, T. and Macy, J.M. (1998). „Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis”. Eur. J. Biochem. 255: 647-653. PMID 9738904.
- ↑ Martin, J.L. (1995). „Thioredoxin - a fold for all reasons”. Structure 3: 245-250. PMID 7788290.
- ↑ Messens, J., Hayburn, G., Desmyter, A., Laus, G. and Wyns, L. (1999). „The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus'”. Biochemistry 38: 16857-16865. PMID 10606519.
- ↑ Radabaugh, T.R. and Aposhian, H.V. (2000). „Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase”. Chem. Res. Toxicol. 13: 26-30. PMID 10649963.
- ↑ Sato, T. and Kobayashi, Y. (1998). „The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite”. J. Bacteriol. 180: 1655-1661. PMID 9537360.
- ↑ Shi, J., Vlamis-Gardikas, V., Aslund, F., Holmgren, A. and Rosen, B.P. (1999). „Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction”. J. Biol. Chem. 274: 36039-36042. PMID 10593884.
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.