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Chemical Compound Review:

MHTP (2S,3R)-3-phosphonooxy-2-(7...

Synonyms: coenzyme B, AC1NUWA4, CHEBI:28890, C04628, 104302-77-4, ...

Kamlage, B. et al., Deppenmeier, U. et al., Noll, K.M. et al., Sauer, F.D. et al.

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High impact information on coenzyme B

The structure of component B of the methylcoenzyme M methylreductase of Methanobacterium thermoautotrophicum was recently assigned as 7-mercaptoheptanoylthreonine phosphate (HS-HTP) (Noll, K [1].
Of various electron donors and acceptors tested, only the reduced form of coenzyme F420 (coenzyme F420H2) and the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate (CoM-S-S-HTP) were capable of reducing and oxidizing the cytochromes at a high rate, respectively [2].
Recently it has been shown that the active site of this cofactor is 7-mercaptoheptanoylthreonine phosphate [3].
This enzyme system exhibits the phenomenon of coupling and uncoupling and represents a different kind of electron transport chain with the heterodisulfide of 2-mercaptoethanesulfonate and 7-mercaptoheptanoylthreonine phosphate as terminal electron acceptor [4].

References

Synthesis of 7-mercaptoheptanoylthreonine phosphate and its activity in the methylcoenzyme M methylreductase system. Noll, K.M., Donnelly, M.I., Wolfe, R.S. J. Biol. Chem. (1987) [Pubmed]
Characterization of cytochromes from Methanosarcina strain Göl and their involvement in electron transport during growth on methanol. Kamlage, B., Blaut, M. J. Bacteriol. (1992) [Pubmed]
Structure of purified cytoplasmic cofactor from Methanobacterium thermoautotrophicum. Sauer, F.D., Blackwell, B.A., Kramer, J.K. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
Reduced coenzyme F420: heterodisulfide oxidoreductase, a proton- translocating redox system in methanogenic bacteria. Deppenmeier, U., Blaut, M., Mahlmann, A., Gottschalk, G. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]

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