Results 251 to 260 of about 1,128,553 (311)
Clinical advancement in the management of mutant isocitrate dehydrogenase (<i>IDH</i>) cancers. [PDF]
EJC SupplBridgewater J +3 more
europepmc +1 more source
Correction to "Succinate Dehydrogenase Pathogenic Variants Among Older Adults With Head and Neck Paragangliomas". [PDF]
Laryngoscope Investig Otolaryngoleuropepmc +1 more source
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Nature, 1961
IT has previously1,2 been reported that there is an enzymatic cycle of inorganic nitrogen. In the present work, we have demonstrated that the dehydrogenating system in the cyclic processes can be separated from the reducing one, and that each dehydrogenase behaves specifically towards different inhibitors.
K, YAMAFUJI, Y, OSAJIMA
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IT has previously1,2 been reported that there is an enzymatic cycle of inorganic nitrogen. In the present work, we have demonstrated that the dehydrogenating system in the cyclic processes can be separated from the reducing one, and that each dehydrogenase behaves specifically towards different inhibitors.
K, YAMAFUJI, Y, OSAJIMA
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Glutamate dehydrogenase-malate dehydrogenase complex
Archives of Biochemistry and Biophysics, 1979Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
L A, Fahien, E, Kmiotek, L, Smith
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2020
Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme secreted by fungi to assist lignocellulolytic enzymes in biomass degradation. Its catalytic flavodehydrogenase (DH) domain is a member of the glucose-methanol-choline oxidoreductase family similar to glucose oxidase.
Florian, Csarman +2 more
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Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme secreted by fungi to assist lignocellulolytic enzymes in biomass degradation. Its catalytic flavodehydrogenase (DH) domain is a member of the glucose-methanol-choline oxidoreductase family similar to glucose oxidase.
Florian, Csarman +2 more
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Annual Review of Microbiology, 1995
Structurally and functionally diverse CO dehydrogenases are key components of various energy-yielding pathways in aerobic and anaerobic microbes from the Bacteria and Archaea domains. Aerobic microbes utilize Mo-Fe-flavin CO dehydrogenases to oxidize CO in respiratory pathways.
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Structurally and functionally diverse CO dehydrogenases are key components of various energy-yielding pathways in aerobic and anaerobic microbes from the Bacteria and Archaea domains. Aerobic microbes utilize Mo-Fe-flavin CO dehydrogenases to oxidize CO in respiratory pathways.
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Stability of dehydrogenases III. malate dehydrogenases
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982Cytoplasmic and mitochondrial malate dehydrogenases from pig and chicken were studied by chemical modification of amino groups, hybridization of immobilization. Determination of thermal stability was used to characterize the different species. Modification of amino groups was found to decrease thermal stability especially when neutralization of the ...
J, Müller, C, Klein
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Biochemical Journal, 2002
The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity ...
Tobias, Modig +2 more
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The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity ...
Tobias, Modig +2 more
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