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J. Biol. Chem., Vol. 277, Issue 16, 13421-13429, April 19, 2002
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From the Department of Biochemistry, Virginia Polytechnic Institute
and State University, Blacksburg, Virginia 24061-0308
The hyperthermophilic euryarchaeon
Methanococcus jannaschii uses coenzyme M
(2-mercaptoethanesulfonic acid) as the terminal methyl carrier in
methanogenesis. We describe an enzyme from that organism,
(2R)-phospho-3-sulfolactate synthase (ComA), that
catalyzes the first step in coenzyme M biosynthesis. ComA catalyzed the stereospecific Michael addition of sulfite to phosphoenolpyruvate over
a broad range of temperature and pH conditions. Substrate and product
analogs moderately inhibited activity. This enzyme has no significant
sequence similarity to previously characterized enzymes; however, its
Mg2+-dependent enzyme reaction mechanism may be
analogous to one proposed for enolase. A diverse group of microbes and
plants have homologs of ComA that could have been recruited for
sulfolactate or sulfolipid biosyntheses.
Identification of Coenzyme M Biosynthetic Phosphosulfolactate
Synthase
A NEW FAMILY OF SULFONATE-BIOSYNTHESIZING ENZYMES*
*
This work was supported by National Science Foundation Grant
MCB 9985712 (to R. H. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biochemistry
(0308), Engel Hall, Virginia Polytechnic Inst. and State University,
Blacksburg, VA 24061-0308. Tel.: 540-231-6605; Fax: 540-231-9070;
E-mail: rhwhite@vt.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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