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6027869 
Journal Article 
Stimulation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase reaction in cell-free extracts of Methanobacterium thermoautotrophicum by the heterodisulfide of coenzyme M and 7-mercapto-heptanoylthreonine phosphate 
Daas, PJH; Keltjens, JT; Kengen, SWM; Vogels, GD; Van Der Drift, C 
1990 
Yes 
Archives of Microbiology
ISSN: 0302-8933
EISSN: 1432-072X 
154 
2 
156-161 
The conversion of formaldehyde to methylcoenzyme M in cell-free extracts of Methanobacterium thermoautotrophicum was stimulated up to 10-fold by catalytic amounts of the heterodisulfide of coenzyme M and 7-mercapto-heptanoylthreonine phosphate. The stimulation required the additional presence of ATP, also in catalytic concentrations. The results described here closely resemble observations made on the activation and reduction of CO sub(2) to formylmethanofuran indicating that this step and the reductive activation of the methyltransferase are controlled by some common mechanism. 
methyltransferase; 7-mercaptoheptanoylthreonine phosphate; Microbiology Abstracts B: Bacteriology; coenzymes; methanobacterium thermoautotrophicum; stimulation; J 02728:Enzymes