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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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Serum isocitric dehydrogenase and glutamic dehydrogenase in schistosomiasis
Transactions of the Royal Society of Tropical Medicine and Hygiene, 1969Abstract 19 patients with schistosomiasis were studied for serum ICDH and GLDH activities; they were divided into two groups according to the presence or absence of hepatic involvement. Serum ICDH levels were normal, except in one patient with advanced hepatic decompensation.
M.S. Shoeb +4 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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2015
Circulating glucocorticoid (GC) levels are controlled by the Hypothalamo-Pituitary-Adrenal (HPA) axis, but within tissues, GC availability is controlled by the isoforms of 11β (Beta)-Hydroxysteroid Dehydrogenase 11β (Beta)-HSD that interconvert inactive cortisone and active cortisol.
Jeremy W. Tomlinson, Conor Woods
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Circulating glucocorticoid (GC) levels are controlled by the Hypothalamo-Pituitary-Adrenal (HPA) axis, but within tissues, GC availability is controlled by the isoforms of 11β (Beta)-Hydroxysteroid Dehydrogenase 11β (Beta)-HSD that interconvert inactive cortisone and active cortisol.
Jeremy W. Tomlinson, Conor Woods
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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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1963
Publisher Summary Dehydrogenases catalyze the hydrogen transfer with pyridine nucleotides as coenzymes. Most of them are involved in the process of biological oxidation and belong to the group that is named “key pathway” enzymes. There exist numerous different apodehydrogenases in human, animal, and plant tissues, most of them catalyze oxidation ...
Werners Ph, Burns Fh
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Publisher Summary Dehydrogenases catalyze the hydrogen transfer with pyridine nucleotides as coenzymes. Most of them are involved in the process of biological oxidation and belong to the group that is named “key pathway” enzymes. There exist numerous different apodehydrogenases in human, animal, and plant tissues, most of them catalyze oxidation ...
Werners Ph, Burns Fh
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Alcohol dehydrogenases, aldehyde dehydrogenases, and related enzymes
Alcohol, 1985Several new structures have recently been determined for dehydrogenases which are involved in alcohol metabolism. These structures give new insight into catalytic properties, structure-function relationships, and evolutionary connections. They also explain the structural basis for known metabolic deviations.
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The Specificity of Dehydrogenases
1980The specificity of dehydrogenases for coenzyme (and coenzyme analogues), and substrate (and substrate analogues) is discussed in relation to structure, function, and evolution. Examples concern compounds that have very different structures, reactions that play widely differing roles in the life of the organism, and organisms of greatly differing types.
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Methanol Dehydrogenase, a PQQ-Containing Quinoprotein Dehydrogenase
2000Methanol dehydrogenase (MDH; EC 1.1.99.8) catalyses the oxidation of methanol to formaldehyde in the periplasm of methylotrophic bacteria during growth on methanol or methane. It was first described in Methylobacterium extorquens (Anthony and Zatman, 1964a,b) and has subsequently been shown to be the one feature that is common to almost all ...
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