منابع مشابه
D-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...
متن کاملHuman Phosphoglycerate Dehydrogenase Produces the Oncometabolite d-2-Hydroxyglutarate
Human d-3-phosphoglycerate dehydrogenase (PHGDH), the first enzyme in the serine biosynthetic pathway, is genomically amplified in tumors including breast cancer and melanoma. In PHGDH-amplified cancer cells, knockdown of PHGDH is not fully rescued by exogenous serine, suggesting possible additional growth-promoting roles for the enzyme. Here we show that, in addition to catalyzing oxidation of...
متن کاملD-serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase.
d-Serine is an endogenous ligand for NMDARs generated from l-serine by the enzyme serine racemase (Srr). Both neuronal and glial localizations have been reported for d-serine and Srr. 3-Phosphoglycerate dehydrogenase is an exclusively astrocytic enzyme that catalyzes the first committed step of l-serine biosynthesis. Using transgenic mice expressing enhanced green fluorescent protein under the ...
متن کاملCofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.
The inhibition of Escherichia coli d-3-phosphoglycerate dehydrogenase by l-serine is positively cooperative with a Hill coefficient of approximately 2, whereas the binding of the inhibitor, l-serine, to the apoenzyme displays positive cooperativity in the binding of the first two serine molecules and negative cooperativity in the binding of the last two serine molecules. An earlier report demon...
متن کاملProbing the regulatory domain interface of D-3-phosphoglycerate dehydrogenase with engineered tryptophan residues.
D-3-Phosphoglycerate dehydrogenase from Escherichia coli is a homotetrameric enzyme which is allosterically regulated by the end product of its pathway, L-serine. The enzyme binds 4 L-serine molecules at two interfaces formed by the noncovalent association of the regulatory domains. The two domains that comprise each interface are related by an approximately 180 degrees axis of symmetry, and tw...
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ژورنال
عنوان ژورنال: Frontiers in Molecular Biosciences
سال: 2018
ISSN: 2296-889X
DOI: 10.3389/fmolb.2018.00110