PMID: 2509421Nov 1, 1989Paper

Transport of coenzyme M (2-mercaptoethanesulfonic acid) and methylcoenzyme M [(2-methylthio)ethanesulfonic acid] in Methanococcus voltae: identification of specific and general uptake systems

Journal of Bacteriology
M Dybas, J Konisky

Abstract

A transport system for coenzyme M (2-mercaptoethanesulfonic acid [HS-CoM]) and methylcoenzyme M [(2-(methylthio)ethanesulfonic acid (CH3-S-CoM)] in Methanococcus voltae required energy, showed saturation kinetics, and concentrated both forms of coenzyme M against a concentration gradient. Transport required hydrogen and carbon dioxide for maximal uptake. CH3-S-CoM uptake was inhibited by N-ethylmaleimide and monensin. Both HS-CoM and CH3-S-CoM uptake showed sodium dependence. In wild-type M. voltae, HS-CoM uptake was concentration dependent, with a Vmax of 960 pmol/min per mg of protein and an apparent Km of 61 microM. Uptake of CH3-S-CoM showed a Vmax of 88 pmol/min per mg of protein and a Km of 53 microM. A mutant of M. voltae resistant to the coenzyme M analog 2-bromoethanesulfonic acid (BES) showed no uptake of CH3-S-CoM but accumulated HS-CoM at the wild-type rate. While the higher-affinity uptake system was specific for HS-CoM, the lower-affinity system mediated uptake of HS-CoM, CH3-S-CoM, and BES. Analysis of the intracellular coenzyme M pools in metabolizing cells showed an intracellular HS-CoM concentration of 14.8 mM and CH3-S-CoM concentration of 0.21 mM.

References

Jan 1, 1979·Journal of Bacteriology·W E Balch, R S Wolfe
Jan 1, 1976·Annual Review of Biochemistry·B C Pressman
May 1, 1989·Applied and Environmental Microbiology·K A Sment, J Konisky
Nov 1, 1974·Journal of Bacteriology·C D TaylorM P Bryant
Mar 1, 1982·Journal of Bacteriology·W B WhitmanR S Wolfe
Apr 1, 1958·Archives of Biochemistry and Biophysics·G L ELLMAN
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Jun 1, 1985·Applied and Environmental Microbiology·D R Lovley
Oct 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·B P CriderJ R Lancaster

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