A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax - type allosteric enzyme
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چکیده
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Discovery of Novel Allosteric Effectors Based on the Predicted Allosteric Sites for Escherichia coli D-3-Phosphoglycerate Dehydrogenase
D-3-phosphoglycerate dehydrogenase (PGDH) from Escherichia coli catalyzes the first critical step in serine biosynthesis, and can be allosterically inhibited by serine. In a previous study, we developed a computational method for allosteric site prediction using a coarse-grained two-state Gō Model and perturbation. Two potential allosteric sites were predicted for E. coli PGDH, one close to the...
متن کاملD-3-Phosphoglycerate Dehydrogenase from Chicken Liver
The molecular weight of chicken liver o-3-phosphoglycerate dehydrogenase, as measured by sedimentation equilibrium analysis, was found to be 165,000, consistent with the measured sedimentation coefficient of 8.13 S. Sedimentation equilibrium studies in 6 M guanidine hydrochloride and gel electrophoresis in sodium dodecyl sulfate gave molecular weights of 40,000 to 43,000, indicating that the pr...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1996
ISSN: 0961-8368
DOI: 10.1002/pro.5560050105