@article {1212,
	title = {Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum.},
	journal = {Extremophiles},
	volume = {11},
	year = {2007},
	month = {2007 Sep},
	pages = {741-6},
	abstract = {<p>Native and recombinant malate dehydrogenase (MDH) was characterized from the hyperthermophilic, facultatively autotrophic archaeon Pyrobaculum islandicum. The enzyme is a homotetramer with a subunit mass of 33 kDa. The activity kinetics of the native and recombinant proteins are the same. The apparent K ( m ) values of the recombinant protein for oxaloacetate (OAA) and NADH (at 80 degrees C and pH 8.0) were 15 and 86 microM, respectively, with specific activity as high as 470 U mg(-1). Activity decreased more than 90\% when NADPH was used. The catalytic efficiency of OAA reduction by P. islandicum MDH using NADH was significantly higher than that reported for any other archaeal MDH. Unlike other archaeal MDHs, specific activity of the P. islandicum MDH back-reaction also decreased more than 90\% when malate and NAD(+) were used as substrates and was not detected with NADP(+). A phylogenetic tree of 31 archaeal MDHs shows that they fall into 5 distinct groups separated largely along taxonomic lines suggesting minimal lateral mdh transfer between Archaea.</p>},
	keywords = {Citric Acid Cycle, Hydrogen-Ion Concentration, Kinetics, Malate Dehydrogenase, Malates, Molecular Weight, NAD, NADP, Oxaloacetic Acid, Phylogeny, Protein Conformation, Protein Subunits, Pyrobaculum, Recombinant Proteins, Sequence Analysis, Protein, Substrate Specificity, Temperature},
	issn = {1431-0651},
	doi = {10.1007/s00792-007-0081-2},
	author = {Yennaco, Lynda J and Hu, Yajing and Holden, James F}
}
@article {872,
	title = {Acetate catabolism in the dissimilatory iron-reducing isolate GS-15.},
	journal = {J Bacteriol},
	volume = {173},
	year = {1991},
	month = {1991 Apr},
	pages = {2704-6},
	abstract = {Acetate-grown GS-15 whole-cell suspensions were disrupted with detergent and assayed for enzymes associated with acetate catabolism. Carbon monoxide dehydrogenase and formate dehydrogenase were not observed in GS-15. Catabolic levels of acetokinase and phosphotransacetylase were observed. Enzyme activities of the citric acid cycle, i.e., isocitrate dehydrogenase, 2-oxoglutarate sythase, succinate dehydrogenase, fumarase, and malate dehydrogenase, were observed.},
	keywords = {Acetate Kinase, Acetates, Acetyl Coenzyme A, Bacteria, Carbon Monoxide, Citric Acid Cycle, Electron Transport, Euryarchaeota, Fumarate Hydratase, Isocitrate Dehydrogenase, Ketone Oxidoreductases, Malate Dehydrogenase, Phosphate Acetyltransferase, Pseudomonas aeruginosa, Succinate Dehydrogenase},
	issn = {0021-9193},
	author = {Champine, J E and Goodwin, S}
}
