@article {1213,
	title = {Citric acid cycle in the hyperthermophilic archaeon Pyrobaculum islandicum grown autotrophically, heterotrophically, and mixotrophically with acetate.},
	journal = {J Bacteriol},
	volume = {188},
	year = {2006},
	month = {2006 Jun},
	pages = {4350-5},
	abstract = {<p>The hyperthermophilic archaeon Pyrobaculum islandicum uses the citric acid cycle in the oxidative and reductive directions for heterotrophic and autotrophic growth, respectively, but the control of carbon flow is poorly understood. P. islandicum was grown at 95 degrees C autotrophically, heterotrophically, and mixotrophically with acetate, H2, and small amounts of yeast extract and with thiosulfate as the terminal electron acceptor. The autotrophic growth rates and maximum concentrations of cells were significantly lower than those in other media. The growth rates on H2 and 0.001\% yeast extract with and without 0.05\% acetate were the same, but the maximum concentration of cells was fourfold higher with acetate. There was no growth with acetate if 0.001\% yeast extract was not present, and addition of H2 to acetate-containing medium greatly increased the growth rates and maximum concentrations of cells. P. islandicum cultures assimilated 14C-labeled acetate in the presence of H2 and yeast extract with an efficiency of 55\%. The activities of 11 of 19 enzymes involved in the central metabolism of P. islandicum were regulated under the three different growth conditions. Pyruvate synthase and acetate:coenzyme A (CoA) ligase (ADP-forming) activities were detected only in heterotrophically grown cultures. Citrate synthase activity decreased in autotrophic and acetate-containing cultures compared to the activity in heterotrophic cultures. Acetylated citrate lyase, acetate:CoA ligase (AMP forming), and phosphoenolpyruvate carboxylase activities increased in autotrophic and acetate-containing cultures. Citrate lyase activity was higher than ATP citrate synthase activity in autotrophic cultures. These data suggest that citrate lyase and AMP-forming acetate:CoA ligase, but not ATP citrate synthase, work opposite citrate synthase to control the direction of carbon flow in the citric acid cycle.</p>},
	keywords = {Acetates, Carbon Dioxide, Citric Acid, Citric Acid Cycle, Culture Media, Deuterium, Ligases, Lyases, Pyrobaculum, Pyruvate Synthase, Substrate Specificity},
	issn = {0021-9193},
	doi = {10.1128/JB.00138-06},
	author = {Hu, Yajing and Holden, James F}
}
@article {669,
	title = {Identification of methyl coenzyme M as an intermediate in methanogenesis from acetate in Methanosarcina spp.},
	journal = {J Bacteriol},
	volume = {160},
	year = {1984},
	month = {1984 Nov},
	pages = {521-5},
	abstract = {The transfer of the methyl group of acetate to coenzyme M (2-mercaptoethanesulfonic acid; HS-CoM) during the metabolism of acetate to methane was investigated in cultures of Methanosarcina strain TM-1. The organism metabolized CD3COO- to 83\% CD3H and 17\% CD2H2 and produced no CDH3 or CH4. The isotopic composition of coenzyme M in cells grown on CD3COO- was analyzed with a novel gas chromatography-mass spectrometry technique. The cells contained CD3-D-CoM and CD2H-S-CoM) in a proportion similar to that of CD3H to CD2H2. These results, in conjunction with a report (J.K. Nelson and J.G. Ferry, J. Bacteriol. 160:526-532, 1984) that extracts of acetate-grown strain TM-1 contain high levels of CH3-S-CoM methylreductase, indicate that CH3-S-CoM is an intermediate in the metabolism of acetate to methane in this organism.},
	keywords = {Acetates, Deuterium, Euryarchaeota, Gas Chromatography-Mass Spectrometry, Mercaptoethanol, Mesna, Methane, Methylation},
	issn = {0021-9193},
	author = {Lovley, D R and White, R H and Ferry, J G}
}
