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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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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 ...
F H, BURNS, P H, WERNERS
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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 ...
F H, BURNS, P H, WERNERS
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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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Lactic Dehydrogenase Electrophoresis
JAMA: The Journal of the American Medical Association, 1968To the Editor:— A recent informative laboratory report ( 205 :294, 1968) reviews the technique of agargel electrophoresis for lactic dehydrogenase isoenzymes. The authors state that the method is simple, so that it can be used in the routine laboratory, requires only about one hour for separation of the isoenzymes, and yields sharp and distinct ...
A W, Opher, C S, Collier, J M, Miller
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Hyperthermophilic dehydrogenase enzymes
Biochemical Society Transactions, 2004Archaeal dehydrogenases are often found to be of a specific class of dehydrogenase which has low sequence identity to the equivalent bacterial and eukaryotic counterparts. This paper focuses on two different types of hyperthermophilic dehydrogenase enzyme that have been cloned and over-expressed in Escherichia coli.
J A, Littlechild, J E, Guy, M N, Isupov
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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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