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Chemical Compound Review

AC1L191M     3-phosphonooxy-2-(7- sulfanylheptanoylamino...

Synonyms: O-phosphono-N-(7-sulfanylheptanoyl)threonine
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High impact information on H-S-CoB

  • All catabolic processes finally lead to the formation of a mixed disulfide from coenzyme M and coenzyme B that functions as an electron acceptor of certain anaerobic respiratory chains [1].
  • Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-S-CoM) with coenzyme B (H-S-CoB) to CH4 and CoM-S-S-CoB in methanogenic archaea [2].
  • The active sites of MCR from M. barkeri and M. kandleri were almost identical to that of M. thermoautotrophicum and predominantly occupied by coenzyme M and coenzyme B [3].
  • Cell-free extracts of these methanogens were shown to carry out the ATP-dependent phosphorylation of N-(7-mercaptoheptanoyl)threonine to HS-HTP [4].
  • MRF contains N-(7-mercaptoheptanoyl)threonine O-3-phosphate (HS-HTP) [No11, K. M., Rinehart, K. L., Tanner, R. S., & Wolfe, R. S. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 4238-4242] and is linked to C-6 of 2-acetamido-2-deoxymannopyranuronic acid of the UDP-disaccharide through a carboxylic-phosphoric anhydride linkage [5].

Biological context of H-S-CoB


Associations of H-S-CoB with other chemical compounds


Gene context of H-S-CoB


  1. The unique biochemistry of methanogenesis. Deppenmeier, U. Prog. Nucleic Acid Res. Mol. Biol. (2002) [Pubmed]
  2. Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: a pulse EPR study. Harmer, J., Finazzo, C., Piskorski, R., Bauer, C., Jaun, B., Duin, E.C., Goenrich, M., Thauer, R.K., Van Doorslaer, S., Schweiger, A. J. Am. Chem. Soc. (2005) [Pubmed]
  3. Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation. Grabarse, W., Mahlert, F., Shima, S., Thauer, R.K., Ermler, U. J. Mol. Biol. (2000) [Pubmed]
  4. Biosynthesis of (7-mercaptoheptanoyl)threonine phosphate. White, R.H. Biochemistry (1994) [Pubmed]
  5. Structure of a novel cofactor containing N-(7-mercaptoheptanoyl)-O-3-phosphothreonine. Sauer, F.D., Blackwell, B.A., Kramer, J.K., Marsden, B.J. Biochemistry (1990) [Pubmed]
  6. Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea. Howell, D.M., Graupner, M., Xu, H., White, R.H. J. Bacteriol. (2000) [Pubmed]
  7. Characterization of the MCRred2 form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study. Finazzo, C., Harmer, J., Jaun, B., Duin, E.C., Mahlert, F., Thauer, R.K., Van Doorslaer, S., Schweiger, A. J. Biol. Inorg. Chem. (2003) [Pubmed]
  8. 7-Mercaptoheptanoylthreonine phosphate functions as component B in ATP-independent methane formation from methyl-CoM with reduced cobalamin as electron donor. Ankel-Fuchs, D., Böcher, R., Thauer, R.K., Noll, K.M., Wolfe, R.S. FEBS Lett. (1987) [Pubmed]
  9. Component C of the methylcoenzyme M methylreductase system contains bound 7-mercaptoheptanoylthreonine phosphate (HS-HTP). Noll, K.M., Wolfe, R.S. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  10. The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states. Mahlert, F., Grabarse, W., Kahnt, J., Thauer, R.K., Duin, E.C. J. Biol. Inorg. Chem. (2002) [Pubmed]
  11. Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum--identification of the catalytic sites for fumarate reduction and thiol oxidation. Heim, S., Künkel, A., Thauer, R.K., Hedderich, R. Eur. J. Biochem. (1998) [Pubmed]
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