Arsenit metiltransferaza

Arsenit metiltransferaza (EC 2.1.1.137, -adenozil--metionin:arsenik(III) metiltransferaza, -adenozil--metionin:metilarsonit -metiltransferaza, metilarsonit metiltransferaza) je enzim sa sistematskim imenom -adenozil--metionin:arsenit -metiltransferaza.^{[1][2][3][4][5]} Ovaj enzim katalizuje sledeću hemijsku reakciju

(1) -adenozil--metionin + arsenit ${\displaystyle \rightleftharpoons }$ -adenozil--homocistein + metilarsonat

(2) -adenozil--metionin + metilarsonit ${\displaystyle \rightleftharpoons }$ -adenozil--homocistein + dimetilarsinat

Arsenit metiltransferaza
Identifikatori
EC broj	2.1.1.137
CAS broj	167140-41-2
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
Pretraga PMC članci PubMed članci NCBI proteini

Ova enzim učestvuje u biotransformacionom putu kojim se formira dimetilarsinat iz nerganskih arsenita i arsenata.

Reference

1. Zakharyan, R.A. & 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.
2. 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.CS1 одржавање: Вишеструка имена: списак аутора (веза)
3. 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.CS1 одржавање: Вишеструка имена: списак аутора (веза)
4. 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.CS1 одржавање: Вишеструка имена: списак аутора (веза)
5. 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.CS1 одржавање: Вишеструка имена: списак аутора (веза)

Literatura

• 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.

Spoljašnje veze

• Arsenite+methyltransferase на ()