Results 381 to 390 of about 1,320,603 (414)
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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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Lactic Dehydrogenase Activity in Blood.∗
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine, 1955Summary and Conclusions 1. Lactic dehydrogenase activity is present in the venous serum of normal human adults. Normal activity ranges from 260 to 850 units per ml with a mean value of470 ± 130 units per ml. 2.
F. Wróblewski, J. S. Ladue
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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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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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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 and cancer: an overview.
Frontiers in Bioscience, 2015Despite the intense scientific efforts made, there are still many tumors that are difficult to treat and the percentage of patient survival in the long-term is still too low. Thus, new approaches to the treatment of cancer are needed.
M. Gallo +5 more
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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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, 2015
Triple mutant K66Q/S149G/N262C (TM_pheDH) of Rhodococcus phenylalanine dehydrogenase (pheDH) was engineered by directed evolution as the first enzyme for the highly enantioselective reductive amination of phenylacetone 1 and 4-phenyl-2-butanone 3, giving
Lidan Ye +5 more
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Triple mutant K66Q/S149G/N262C (TM_pheDH) of Rhodococcus phenylalanine dehydrogenase (pheDH) was engineered by directed evolution as the first enzyme for the highly enantioselective reductive amination of phenylacetone 1 and 4-phenyl-2-butanone 3, giving
Lidan Ye +5 more
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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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