Arsenit metiltransferaza
(Preusmjereno sa stranice EC 2.1.1.137)
| Arsenit metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.137 | ||||||||
| CAS broj | 167140-41-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Arsenit metiltransferaza (EC 2.1.1.137, S-adenozil-L-metionin:arsenik(III) metiltransferaza, S-adenozil-L-metionin:metilarsonit As-metiltransferaza, metilarsonit metiltransferaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:arsenit As-metiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) S-adenozil-L-metionin + arsenit S-adenozil-L-homocistein + metilarsonat
- (2) S-adenozil-L-metionin + metilarsonit S-adenozil-L-homocistein + dimetilarsinat
Ova enzim učestvuje u biotransformacionom putu kojim se formira dimetilarsinat iz nerganskih arsenita i arsenata.
Reference[uredi | uredi kod]
- ↑ Zakharyan, R.A. and Aposhian, H.V. (1999). „Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase”. Chem. Res. Toxicol. 12: 1278-1283. PMID 10604879.
- ↑ Zakharyan, R.A., Ayala-Fierro, F., Cullen, W.R., Carter, D.M. and Aposhian, H.V. (1999). „Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes”. Toxicol. Appl. Pharmacol. 158: 9-15. PMID 10387927.
- ↑ Zakharyan, R.A., Wildfang, E. and Aposhian, H.V. (1996). „Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkeys are deficient in methyltransferases that methylate inorganic arsenic”. Toxicol. Appl. Pharmacol. 140: 77-84. PMID 8806872.
- ↑ Zakharyan, R.A., Wu, Y., Bogdan, G.M. and Aposhian, H.V. (1995). „Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver”. Chem. Res. Toxicol. 8: 1029-1038. PMID 8605285.
- ↑ Lin, S., Shi, Q., Nix, F.B., Styblo, M., Beck, M.A., Herbin-Davis, K.M., Hall, L.L., Simeonsson, J.B. and Thomas, D.J. (2002). „A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol”. J. Biol. Chem. 277: 10795-10803. PMID 11790780.
Literatura[uredi | uredi kod]
- 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.