JBC Transcription and Nuclear Factor Monoclonals

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mozier, N. M.
Right arrow Articles by Hoffman, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mozier, N. M.
Right arrow Articles by Hoffman, J. L.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 263, Issue 10, 4527-4531, 04, 1988

S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism

NM Mozier, KP McConnell and JL Hoffman
Department of Biochemistry, University of Louisville, Kentucky 40292.

The final urinary excretion product of selenium detoxification is trimethylselenonium ion. An assay has been developed for the enzyme, S- adenosylmethionine:thioether S-methyltransferase, responsible for this final methylation reaction. This assay employed high pressure liquid chromatography separation and quantitation of the trimethylselenonium ion produced by thioether methyltransferase acting on S- adenosylmethionine and dimethyl selenide. The enzyme was shown to reside primarily in the cytosol of mouse lung (30 pmol/mg protein/min) and liver (7 pmol/mg protein/min). Purification from mouse lung to a preparation that exhibited a single band on sodium dodecyl sulfate- polyacrylamide gel electrophoresis was achieved by DEAE, gel filtration, and chromatofocusing chromatographies. Thioether methyltransferase is monomeric with a molecular weight of 28,000 and has a pI of 5.3. The pH optimum was 6.3, and Km values for dimethyl selenide and S-adenosylmethionine were 0.4 and 1.0 microM, respectively. The enzyme was inhibited 50% by 25 microM sinefungin, an analog of S-adenosylmethionine, or 40 microM S-adenosylhomocysteine, the reaction product. Pure thioether methyltransferase methylated selenium in dimethyl selenide, tellurium in dimethyl telluride, and S in dimethyl sulfide and many other thioethers. These data suggest a general role for this novel enzyme in the synthesis of onium compounds with increased aqueous solubility helpful in their excretion.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Physiol. GenomicsHome page
M. Ding and L. A. Toth
mRNA expression in mouse hypothalamus and basal forebrain during influenza infection: a novel model for sleep regulation
Physiol Genomics, February 23, 2006; 24(3): 225 - 234.
[Abstract] [Full Text] [PDF]


Home page
Physiol. GenomicsHome page
M. Bauer, A. C. Hamm, M. Bonaus, A. Jacob, J. Jaekel, H. Schorle, M. J. Pankratz, and J. D. Katzenberger
Starvation response in mouse liver shows strong correlation with life-span-prolonging processes
Physiol Genomics, April 13, 2004; 17(2): 230 - 244.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Lin, Q. Shi, F. B. Nix, M. Styblo, M. A. Beck, K. M. Herbin-Davis, L. L. Hall, J. B. Simeonsson, and D. J. Thomas
A Novel S-Adenosyl-L-methionine:Arsenic(III) Methyltransferase from Rat Liver Cytosol
J. Biol. Chem., March 22, 2002; 277(13): 10795 - 10803.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. Neuhierl, M. Thanbichler, F. Lottspeich, and A. Bock
A Family of S-Methylmethionine-dependent Thiol/Selenol Methyltransferases. ROLE IN SELENIUM TOLERANCE AND EVOLUTIONARY RELATION
J. Biol. Chem., February 26, 1999; 274(9): 5407 - 5414.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1988 by the American Society for Biochemistry and Molecular Biology.