Results 41 to 50 of about 23,057 (164)
Frontiers in Plant Science, 2018 The phosphorylated pathway of serine biosynthesis represents an important pathway in plants. The pathway consist of three reactions catalyzed by the phosphoglycerate dehydrogenase, the phosphoserine aminotransferase and the phosphoserine phosphatase, and
Sabine Wulfert, Stephan Krueger
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A novel small-molecule inhibitor of 3-phosphoglycerate dehydrogenase. [PDF]
Mol Cell Oncol, 2016 Serine metabolism is likely to play a critical role in cancer cell growth. A recent study reports the identification of a novel small-molecule inhibitor of serine synthesis that targets 3-phosphoglycerate dehydrogenase (PHGDH), the first enzyme of the serine synthesis pathway, and selectively abrogates the proliferation of PHGDH overexpressing breast ...
Mullarky E +3 more
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Inhibition of 3-phosphoglycerate dehydrogenase by
Biochemical Journal, 1968 1. l-Serine was shown to be a highly specific inhibitor of 3-phosphoglycerate dehydrogenase. 2. 3-Phosphoglycerate dehydrogenase is cold-labile with respect to its catalytic activity and to sensitivity to serine. 3. l-Serine protects the catalytic site as well as the inhibitor site. 4. Glycerol protects the catalytic site as well as the inhibitor site.
J C, Slaughter, D D, Davies
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Proteomics analysis of antimalarial targets of Garcinia mangostana Linn.
Asian Pacific Journal of Tropical Biomedicine, 2014 Objective: To investigate possible protein targets for antimalarial activity of Garcinia mangostana Linn. (G. mangostana) (pericarp) in 3D7 Plasmodium falciparum clone using 2-dimensional electrophoresis and liquid chromatography mass-spectrometry (LC/MS/
Wanna Chaijaroenkul +4 more
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The malate-aspartate shuttle is important for de novo serine biosynthesis
Cell Reports, 2023 Summary: The malate-aspartate shuttle (MAS) is a redox shuttle that transports reducing equivalents across the inner mitochondrial membrane while recycling cytosolic NADH to NAD+.
Melissa H. Broeks +11 more
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Probing Subunit Interactions in 3‐Phosphoglycerate Dehydrogenase
The FASEB Journal, 2012 3‐Phosphoglycerate Dehydrogenase is a homotetramer with three types of subunit interfaces; between adjacent regulatory domains, cofactor domains, and across the central cavity of the tetramer. A single tryptophan per subunit lies at the cofactor interface and crosses over between adjacent subunits.
Falk, Bradley, Bell, Ellis
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Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases [PDF]
Archives of Biochemistry and Biophysics, 2012 D-3-Phosphoglycerate dehydrogenases (PGDH) exist with at least three different structural motifs and the enzymes from different species display distinctly different mechanisms. In many species, particularly bacteria, the catalytic activity is regulated allosterically through binding of l-serine to a distinct structural domain, termed the ACT domain ...
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Proteomes, 2014 The present study was performed to unravel the mechanisms of systemic acquired resistance (SAR) establishment and resistance signaling pathways against the canker-rot fungus (Inonotus obliquus strain IO-U1) infection in Japanese birch plantlet No.8 ...
Hiromu Suzuki +4 more
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FEBS Letters, EarlyView.We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee +3 more
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The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas [PDF]
Biochemical Journal, 1968 1. 3-Phosphoglycerate dehydrogenase was purified 400-fold from crude extracts of etiolated pea epicotyls. 2. Michaelis constants were determined for all four substrates. 3. Loss of sensitivity to inhibition by l-serine occurs on purification. 4. The purified enzyme is inhibited by thiol-group reagents and, with N-ethyl-maleimide, protection is afforded
J C, Slaughter, D D, Davies
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