Results 11 to 20 of about 45,633 (272)
The obligate intracellular pathogen, Anaplasma phagocytophilum, is the causative agent of life-threatening diseases in humans and animals. A. phagocytophilum is an emerging tick-borne pathogen in the United States, Europe, Africa and Asia, with ...
Alejandro Cabezas-Cruz +7 more
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The xylulose 5-phosphate/phosphate translocator (PTs) (XPT) represents a link between the plastidial and extraplastidial branches of the oxidative pentose phosphate pathway. Its role is to retrieve pentose phosphates from the extraplastidial space and to
Elke J. A. Hilgers +4 more
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Background Cyanobacteria are promising hosts for the production of various industrially important compounds such as succinate. This study focuses on introduction of the glyoxylate shunt, which is naturally present in only a few cyanobacteria, into ...
Claudia Durall +5 more
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An in vitro Coupled Assay for PEPC with Control of Bicarbonate Concentration
Phosphoenolpyruvate carboxylase (PEPC) catalyzes a critical step in carbon metabolism in plants and bacteria, the irreversible reaction between bicarbonate and phosphoenolpyruvate to produce the C4 compound oxaloacetate.
Nicholas Moody +2 more
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The NADPH oxidase NOX4 regulates redox and metabolic homeostasis preventing HCC progression
Loss of NOX4 in HCC tumor cells induces metabolic reprogramming in a Nrf2/MYC‐dependent manner to promote HCC progression. Abstract Background and Aims The NADPH oxidase NOX4 plays a tumor‐suppressor function in HCC. Silencing NOX4 confers higher proliferative and migratory capacity to HCC cells and increases their in vivo tumorigenic potential in ...
Irene Peñuelas‐Haro +14 more
wiley +1 more source
Regulation at the Phosphoenolpyruvate Branchpoint in Azotobacter vinelandii : Phosphoenolpyruvate Carboxylase [PDF]
Phosphoenolpyruvate carboxylase (EC 4.1.1.31) from Azotobacter vinelandii , like the corresponding enzyme from other organisms, is activated by acetyl coenzyme A and inhibited by l -aspartate. Both modifiers affect primarily the affinity of the enzyme for phosphoenolpyruvate.
C L, Liao, D E, Atkinson
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Cloning and expression of phosphoenolpyruvate carboxykinase from Escherichia coli
In order to better study the structure and function of phosphoenolpyruvate carboxylase, the phosphoenolpyruvate carboxylase gene is cloned and expressed by PCR (polymerase chain reaction), double enzyme digestion and cell transformation. The results show
Xiaoliang HE +6 more
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Existing types of muscles differ not only structurally, but also metabolically (direction of energy exchange, choice of biosubstrates, dependence on the action of mediators, hormones, etc.).
G. Stepanov +3 more
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Abstract The optically pure d and l isomers of 2-phospholactate were synthesized by phosphorylation of the appropriate lactic acids. The interactions of these analogues and of phosphoglycolate with several enzymes that catalyze reactions of phosphoenolpyruvate were examined by kinetics and by direct binding studies measuring the longitudinal relaxation
T, Nowak, A S, Mildvan
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Biological Evaluation of a Mitochondrial Phosphoenolpyruvate Carboxykinase Inhibitor
Phosphoenolpyruvate carboxykinase (PEPCK) is a key enzyme in gluconeogenesis, catalyzingthe decarboxylation of oxaloacetate to phosphoenolpyruvate. [...]
Sergio Rodríguez-Arévalo +9 more
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