| A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol. | |
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MedLine Citation:
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PMID: 11790780 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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S-Adenosyl-l-methionine (AdoMet):arsenic(III) methyltransferase, purified from liver cytosol of adult male Fischer 344 rats, catalyzes transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. The kinetics of production of methylated arsenicals in reaction mixtures containing enzyme, AdoMet, dithiothreitol, glutathione (GSH), and arsenite are consistent with a scheme in which monomethylated arsenical produced from arsenite is the substrate for a second methylation reaction that yields dimethylated arsenical. The mRNA for this protein predicts a 369-amino acid residue protein (molecular mass 41056) that contains common methyltransferase sequence motifs. Its sequence is similar to Cyt19, a putative methyltransferase, expressed in human and mouse tissues. Reverse transcription-polymerase chain reaction detects S-adenosyl-l-methionine:arsenic(III) methyltransferase mRNA in rat tissues and in HepG2 cells, a human cell line that methylates arsenite and methylarsonous acid. S-Adenosyl-l-methionine:arsenic(III) methyltransferase mRNA is not detected in UROtsa cells, an immortalized human urothelial cell line that does not methylate arsenite. Because methylation of arsenic is a critical feature of its metabolism, characterization of this enzyme will improve our understanding of this metalloid's metabolism and its actions as a toxin and a carcinogen. |
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Authors:
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Shan Lin; Qing Shi; F Brent Nix; Miroslav Styblo; Melinda A Beck; Karen M Herbin-Davis; Larry L Hall; Josef B Simeonsson; David J Thomas |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. Date: 2002-01-14 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 277 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2002 Mar |
Date Detail:
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Created Date: 2002-03-25 Completed Date: 2002-05-10 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 10795-803 Citation Subset: IM |
Affiliation:
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Curriculum in Toxicology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/AF393243 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Base Sequence Cell Line, Transformed Chromatography, Gel Cytosol / enzymology* DNA, Complementary Humans Kinetics Liver / enzymology* Male Methyltransferases / chemistry, genetics, isolation & purification*, metabolism Molecular Sequence Data RNA, Messenger / genetics, metabolism Rats Rats, Inbred F344 Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Substrate Specificity |
| Grant Support | |
ID/Acronym/Agency:
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DK56350/DK/NIDDK NIH HHS; ES09941/ES/NIEHS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/DNA, Complementary; 0/RNA, Messenger; EC 2.1.1.-/Methyltransferases; EC 2.1.1.-/S-adenosyl-L-methionine arsenic(III) methyltransferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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