Inhibition by corrins of the ATP-dependent activation and CO2 reduction by the methylreductase system in Methanobacterium bryantii.
Corrins inhibited the ATP-dependent activation of the methylreductase system and the methyl coenzyme M-dependent reduction of CO2 in extracts of Methanobacterium bryantii resolved from low-molecular-weight factors. The concentrations of cobinamides and cobamides required for one-half of maximal inhibition of the ATP-dependent activation were between 1 and 5 microM. Cobinamides were more inhibitory at lower concentrations than cobamides. Deoxyadenosylcobalamin was not inhibitory at concentrations up to 25 microM. The inhibition of CO2 reduction was competitive with respect to CO2. The concentration of methylcobalamin required for one-half of maximal inhibition was 5 microM. Other cobamides inhibited at similar concentrations, but diaquacobinamide inhibited at lower concentrations. With respect to their affinities and specificities for corrins, inhibition of both the ATP-dependent activation and CO2 reduction closely resembled the corrin-dependent activation of the methylreductase described in similar extracts (W. B. Whitman and R. S. Wolfe, J. Bacteriol. 164:165-172, 1985). However, whether the multiple effects of corrins are due to action at a single site is unknown.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D002245:Carbon Dioxide / Q000378:metabolism*; D003038:Cobamides / Q000494:pharmacology*; D004789:Enzyme Activation; D019605:Euryarchaeota / Q000201:enzymology*; D010088:Oxidoreductases / Q000378:metabolism*; D010728:Phosphoenolpyruvate / Q000494:pharmacology; D014805:Vitamin B 12 / Q000031:analogs & derivatives / Q000494:pharmacology
D003038:Cobamides; C017142:cobinamide; D002245:Carbon Dioxide; D010728:Phosphoenolpyruvate; D000255:Adenosine Triphosphate; C019476:mecobalamin; D010088:Oxidoreductases; C023895:methyl coenzyme M methylreductase; D014805:Vitamin B 12