Show simple item record

dc.contributor.authorPartovi, Sarah E.
dc.contributor.authorMus, Florence
dc.contributor.authorGutknecht, Andrew E.
dc.contributor.authorMartinez, Hunter A.
dc.contributor.authorTripet, Brian P.
dc.contributor.authorLange, Bernd Markus
dc.contributor.authorDuBois, Jennifer L.
dc.contributor.authorPeters, John W.
dc.date.accessioned2018-07-23T23:24:34Z
dc.date.available2018-07-23T23:24:34Z
dc.date.issued2018-04
dc.identifier.citationPartovi, Sarah E. , Florence Mus, Andrew E. Gutknecht, Hunter A. Martinez, Brian P. Tripet, Bernd Markus Lange, Jennifer L. DuBois, and John W. Peters. "Coenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamily." The Journal of Biological Chemistry (February 2018). DOI: 10.1074/jbc.RA117.001234.en_US
dc.identifier.issn1083-351X
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/14665
dc.description.abstractFor nearly 30 years, coenzyme M (CoM) was assumed to be present solely in methanogenic archaea. In the late 1990s, CoM was reported to play a role in bacterial propene metabolism, but no biosynthetic pathway for CoM has yet been identified in bacteria. Here, using bioinformatics and proteomic approaches in the metabolically versatile bacterium Xanthobacter autotrophicus Py2, we identified four putative CoM biosynthetic enzymes encoded by xcbB1, C1, D1, and E1 genes. Only XcbB1 was homologous to a known CoM biosynthetic enzyme (ComA), indicating that CoM biosynthesis in bacteria involves enzymes different from those in archaea. We verified that the ComA homolog produces phosphosulfolactate from phosphoenolpyruvate (PEP), demonstrating that bacterial CoM biosynthesis is initiated similarly to the PEP-dependent methanogenic archaeal pathway. The bioinformatics analysis revealed that XcbC1 and D1 are members of the aspartase/fumarase superfamily (AFS) and that XcbE1 is a pyridoxal 5\'-phosphate-containing enzyme with homology to D-cysteine desulfhydrases. Known AFS members catalyze beta-elimination reactions of succinyl-containing substrates, yielding fumarate as the common unsaturated elimination product. Unexpectedly, we found that XcbC1 catalyzes beta-elimination on phosphosulfolactate, yielding inorganic phosphate and a novel metabolite, sulfoacrylic acid. Phosphate-releasing beta-elimination reactions are unprecedented among the AFS, indicating that XcbC1 is an unusual phosphatase. Direct demonstration of phosphosulfolactate synthase activity for XcbB1 and phosphate beta-elimination activity for XcbC1 strengthened their hypothetical assignment to a CoM biosynthetic pathway and suggested functions also for XcbD1 and E1. Our results represent a critical first step toward elucidating the CoM pathway in bacteria.en_US
dc.description.sponsorshipDepartment of Energy, Office of Science, Office of Basic Energy Sciences under Award Number DE-FG02-04ER15563en_US
dc.language.isoenen_US
dc.rightsThis Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).en_US
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en_US
dc.titleCoenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamilyen_US
dc.typeArticleen_US
mus.citation.extentfirstpage5236en_US
mus.citation.extentlastpage5246en_US
mus.citation.journaltitleJournal of Biological Chemistryen_US
mus.citation.volume293en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1074/jbc.RA117.001234en_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage3en_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record