Table of Contents Author Guidelines Submit a Manuscript
Archaea
Volume 2017 (2017), Article ID 5793620, 6 pages
https://doi.org/10.1155/2017/5793620
Research Article

Expression, Purification, and Characterization of (R)-Sulfolactate Dehydrogenase (ComC) from the Rumen Methanogen Methanobrevibacter millerae SM9

AgResearch Limited, Grasslands Research Centre, Tennent Drive, Private Bag 11008, Palmerston North 4442, New Zealand

Correspondence should be addressed to Linley R. Schofield; zn.oc.hcraeserga@dleifohcs.yelnil

Received 10 May 2017; Accepted 19 September 2017; Published 6 November 2017

Academic Editor: Nils-Kåre Birkeland

Copyright © 2017 Yanli Zhang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. D. E. Graham and R. H. White, “Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics,” Natural Product Reports, vol. 19, no. 2, pp. 133–147, 2002. View at Publisher · View at Google Scholar · View at Scopus
  2. D. E. Graham, “2-oxoacid metabolism in methanogenic CoM and CoB biosynthesis,” Methods in Enzymology, vol. 494, pp. 301–326, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. W. E. Balch and R. S. Wolfe, “Transport of coenzyme M (2-mercaptoethanesulfonic acid) in Methanobacterium ruminantium,” Journal of Bacteriology, vol. 137, no. 1, pp. 264–273, 1979. View at Google Scholar
  4. C. E. Hand and J. F. Honek, “Biological chemistry of naturally occurring thiols of microbial and marine origin,” Journal of Natural Products, vol. 68, no. 2, pp. 293–308, 2005. View at Publisher · View at Google Scholar · View at Scopus
  5. N. Santoro and J. Konisky, “Characterization of bromoethanesulfonate-resistant mutants of Methanococcus voltae: evidence of a coenzyme M transport system,” Journal of Bacteriology, vol. 169, no. 2, pp. 660–665, 1987. View at Publisher · View at Google Scholar
  6. Y. Liu, L. L. Beer, and W. B. Whitman, “Sulfur metabolism in archaea reveals novel processes,” Environmental Microbiology, vol. 14, no. 10, pp. 2632–2644, 2012. View at Publisher · View at Google Scholar · View at Scopus
  7. D. E. Graham, M. Graupner, H. Xu, and R. H. White, “Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase: a member of a new class of Mg2+-dependent acid phosphatases,” European Journal of Biochemistry, vol. 268, no. 19, pp. 5176–5188, 2001. View at Publisher · View at Google Scholar · View at Scopus
  8. M. Graupner and R. H. White, “The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea,” Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1548, no. 1, pp. 169–173, 2001. View at Publisher · View at Google Scholar · View at Scopus
  9. M. Graupner, H. Xu, and R. H. White, “Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M,” Journal of Bacteriology, vol. 182, no. 17, pp. 4862–4867, 2000. View at Publisher · View at Google Scholar · View at Scopus
  10. A. Irimia, D. Madern, G. Zaccaï, and F. M. Vellieux, “Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes,” The EMBO Journal, vol. 23, no. 6, pp. 1234–1244, 2004. View at Publisher · View at Google Scholar · View at Scopus
  11. M. Graupner, H. Xu, and R. H. White, “Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea,” Journal of Bacteriology, vol. 182, no. 13, pp. 3688–3692, 2000. View at Publisher · View at Google Scholar · View at Scopus
  12. H. Muramatsu, H. Mihara, M. Goto et al., “A new family of NAD(P)H-dependent oxidoreductases distinct from conventional Rossmann-fold proteins,” Journal of Bioscience and Bioengineering, vol. 99, no. 6, pp. 541–547, 2005. View at Publisher · View at Google Scholar · View at Scopus
  13. C. R. Goward and D. J. Nicholls, “Malate dehydrogenase: a model for structure, evolution, and catalysis,” Protein Science, vol. 3, no. 10, pp. 1883–1888, 1994. View at Publisher · View at Google Scholar
  14. K. D. Allen and R. H. White, “Occurrence and biosynthesis of 3-mercaptopropionic acid in Methanocaldococcus jannaschii,” FEMS Microbiology Letters, vol. 363, no. 19, 2016. View at Publisher · View at Google Scholar · View at Scopus
  15. E. Honka, S. Fabry, T. Niermann, P. Palm, and R. Hensel, “Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus,” European Journal of Biochemistry, vol. 188, no. 3, pp. 623–632, 1990. View at Publisher · View at Google Scholar · View at Scopus
  16. H. Thompson, A. Tersteegen, R. K. Thauer, and R. Hedderich, “Two malate dehydrogenases in Methanobacterium thermoautotrophicum,” Archives of Microbiology, vol. 170, no. 1, pp. 38–42, 1998. View at Publisher · View at Google Scholar · View at Scopus
  17. D. E. Graham, S. M. Taylor, R. Z. Wolf, and S. C. Namboori, “Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase,” Biochemical Journal, vol. 424, no. 3, pp. 467–478, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Denger and A. M. Cook, “Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase,” Microbiology, vol. 156, no. 3, pp. 967–974, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. G. Henderson, F. Cox, S. Kittelmann et al., “Effect of DNA extraction methods and sampling techniques on the apparent structure of cow and sheep rumen microbial communities,” PLoS One, vol. 8, no. 9, 2013. View at Publisher · View at Google Scholar
  20. T. Knight, R. S. Ronimus, D. Dey et al., “Chloroform decreases rumen methanogenesis and methanogen populations without altering rumen function in cattle,” Animal Feed Science and Technology, vol. 166-167, pp. 101–112, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. W. J. Kelly, D. M. Pacheco, D. Li, G. T. Attwood, E. Altermann, and S. C. Leahy, “The complete genome sequence of the rumen methanogen Methanobrevibacter millerae SM9,” Standards in Genomic Sciences, vol. 11, no. 1, 2016. View at Publisher · View at Google Scholar · View at Scopus
  22. K. R. Lassey, “Livestock methane emission and its perspective in the global methane cycle,” Australian Journal of Experimental Agriculture, vol. 48, no. 2, pp. 114–118, 2008. View at Publisher · View at Google Scholar · View at Scopus
  23. L. R. Schofield, A. K. Beattie, C. M. Tootill, D. Dey, and R. S. Ronimus, “Biochemical characterisation of phage pseudomurein endoisopeptidases PeiW and PeiP using synthetic peptides,” Archaea, vol. 2015, Article ID 828693, 12 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  24. R. J. Leatherbarrow, GraFit Version 7, Erithacus Software Ltd., Horley, UK, 2009.
  25. R. A. Kohn and T. F. Dunlap, “Calculation of the buffering capacity of bicarbonate in the rumen and in vitro,” Journal of Animal Science, vol. 76, no. 6, pp. 1702–1709, 1998. View at Publisher · View at Google Scholar
  26. S. C. Leahy, W. J. Kelly, E. Altermann et al., “The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions,” PLoS One, vol. 5, no. 1, 2010. View at Publisher · View at Google Scholar
  27. D. R. Lovley, R. C. Greening, and J. G. Ferry, “Rapidly growing rumen methanogenic organism that synthesizes coenzyme M and has a high affinity for formate,” Applied and Environmental Microbiology, vol. 48, no. 1, pp. 81–87, 1984. View at Google Scholar