Results 301 to 310 of about 1,224,293 (342)
Omics Analysis of Lignin Degradation by the Gut Microbiomes of Wood-Eating Hypomeces squamosus Fabricius. [PDF]
MicrobiologyopenMao C, Zhang Q, Zhang J, Li X.
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Endosymbiosis in trypanosomatids: the bacterium regulates the intermediate and oxidative metabolism of the host cell. [PDF]
mSphereBarrinha A +7 more
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Classical Hodgkin lymphoma associated with immune deficiency and dysregulation exhibits a prognosis similar to sporadic cases but with distinct predictive markers. [PDF]
Ann HematolMukae J +13 more
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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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