@article {1208,
	title = {Production of hydrogen from α-1,4- and β-1,4-linked saccharides by marine hyperthermophilic Archaea.},
	journal = {Appl Environ Microbiol},
	volume = {77},
	year = {2011},
	month = {2011 May},
	pages = {3169-73},
	abstract = {<p>Nineteen hyperthermophilic heterotrophs from deep-sea hydrothermal vents, plus the control organism Pyrococcus furiosus, were examined for their ability to grow and produce H$_{2}$ on maltose, cellobiose, and peptides and for the presence of the genes encoding proteins that hydrolyze starch and cellulose. All of the strains grew on these disaccharides and peptides and converted maltose and peptides to H$_{2}$ even when elemental sulfur was present as a terminal electron acceptor. Half of the strains had at least one gene for an extracellular starch hydrolase, but only P. furiosus had a gene for an extracellular β-1,4-endoglucanase. P. furiosus was serially adapted for growth on CF11 cellulose and H$_{2}$ production, which is the first reported instance of hyperthermophilic growth on cellulose, with a doubling time of 64 min. Cell-specific H$_{2}$ production rates were 29 fmol, 37 fmol, and 54 fmol of H$_{2}$ produced cell$^{-}${\textonesuperior} doubling$^{-}${\textonesuperior} on α-1,4-linked sugars, β-1,4-linked sugars, and peptides, respectively. The highest total community H$_{2}$ production rate came from growth on starch (2.6 mM H$_{2}$ produced h$^{-}${\textonesuperior}). Hyperthermophilic heterotrophs may serve as an important alternate source of H$_{2}$ for hydrogenotrophic microorganisms in low-H$_{2}$ hydrothermal environments, and some are candidates for H$_{2}$ bioenergy production in bioreactors.</p>},
	keywords = {Archaea, Carbohydrate Metabolism, Hot Springs, Hydro-Lyases, Hydrogen, Peptides, Seawater},
	issn = {1098-5336},
	doi = {10.1128/AEM.01366-10},
	author = {Oslowski, Daniel M and Jung, Jong-Hyun and Seo, Dong-Ho and Park, Cheon-Seok and Holden, James F}
}
@article {1714,
	title = {[Intermediate plateaux in kinetics of the reaction catalyzed by biodegradative L-threonine dehydratase from Escherichia coli].},
	journal = {Biokhimiia},
	volume = {40},
	year = {1975},
	month = {1975 May-Jun},
	pages = {645-51},
	abstract = {<p>It has been shown that for the reaction catalyzed by "biodegradative" L-threonine dehydratase from E. coli strains K-12 and 980 in 0.5 M phosphate-carbonate buffer, pH 8.4 and pH 9.5, the plots of initial reaction rate (v) versus the initial substrate concentration ([S]0 are characterized by several inflection points, i. e. an intermediate plateau. The plot of v versus the allosteric activator (AMP) concentration have very complicated shapes: there are several inflection points, and also the maximum at L-threonine concentration equal to 3-10(2) and 5-10(-2) M. High AMP concentrations inhibit the enzyme at high substrate concentrations. The reduced glutathion dose not influence the enzyme and does not alter the activating effect of AMP. On the basis of the data obtained it is proposed that the substrate and AMP shift the equilibrium between multiple oligomeric enzyme forms differing in catalytic activity and kinetic manifestations of allosteric interactions between the active and allosteric AMP-binding sites towards polymerization. Thus, the functioning the enzyme under study is discussed in the frames of the model of dissociating regulatory enzymes with multiple intermediate oligomeric forms.</p>},
	keywords = {Adenosine Monophosphate, Allosteric Regulation, Allosteric Site, Binding Sites, Escherichia coli, Hydro-Lyases, Hydrogen-Ion Concentration, Kinetics, Protein Binding, Threonine Dehydratase},
	issn = {0320-9725},
	author = {Sinelnikova, E M and Dvoretskova, T V and Kagan, Z S}
}
