Results 311 to 320 of about 1,224,293 (342)
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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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Alcohol dehydrogenases and aldehyde dehydrogenases
Biochemical Society Transactions, 1988HANS JÖRNVALL +6 more
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Lactate dehydrogenase isoenzymes
Journal of Chromatography B: Biomedical Sciences and Applications, 1988The analytical procedures for LD isoenzymes include electrophoresis, chromatography, immunochemical and kinetic methods. Electrophoretic methods are generally preferred because the resulting patterns are directly observable and all five isoenzymes are resolved in a single procedure.
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Biochemical and Biophysical Research Communications, 1962
M R, RAO, W W, ALTEKAR
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M R, RAO, W W, ALTEKAR
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