Arsenat reduktaza (glutaredoksin)
Изглед
Arsenat reduktaza (glutaredoksin) | |||||||||
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Identifikatori | |||||||||
EC broj | 1.20.4.1 | ||||||||
CAS broj | 146907-46-2 | ||||||||
Baze podataka | |||||||||
IntEnz | IntEnz pregled | ||||||||
BRENDA | BRENDA pristup | ||||||||
ExPASy | NiceZyme pregled | ||||||||
KEGG | KEGG pristup | ||||||||
MetaCyc | metabolički put | ||||||||
PRIAM | profil | ||||||||
Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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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 + glutaredoksin arsenit + glutaredoksin disulfid + H2O
Ovaj enzim je molibdoenzim.
Reference
[уреди | уреди извор]- ^ 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. & 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. & 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. & 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. & 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
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
[уреди | уреди извор]- Arsenate+reductase+(glutaredoxin) на US National Library of Medicine Medical Subject Headings (MeSH)