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Gene Review

UTI89_C3974  -  phosphoglycerate dehydrogenase

Escherichia coli UTI89

 
 
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Disease relevance of UTI89_C3974

 

High impact information on UTI89_C3974

  • They reveal that PGDH displays half-of-the-sites activity with respect to its active sites and that the two sites that are active at any particular time lie in subunits on either side of the nucleotide binding domain interface [3].
  • D-3-Phosphoglycerate dehydrogenase (PGDH) from Escherichia coli is allosterically inhibited by L-serine, the end product of its metabolic pathway [4].
  • 3-Phosphoglycerate dehydrogenase (PGDH), the first enzyme that is involved in the phosphorylated pathway of Ser biosynthesis, is responsible for the oxidation of 3-phosphoglycerate to phosphohydroxypyruvate [5].
  • Southern hybridization analysis and restriction fragment length polymorphism mapping indicated that PGDH is a single-copy gene that is mapped to the upper arm of chromosome 1 [5].
  • These consist of a group of cationic residues (Arg-240, Arg-60, Arg-62, Lys-39, and Lys-141') that potentially form an electrostatic environment for the binding of the negatively charged substrate, as well as the only tryptophan residue found in PGDH and which fits into a hydrophobic pocket immediately adjacent to the active site histidine residue [4].
 

Chemical compound and disease context of UTI89_C3974

 

Biological context of UTI89_C3974

 

Associations of UTI89_C3974 with chemical compounds

 

Analytical, diagnostic and therapeutic context of UTI89_C3974

References

  1. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Schuller, D.J., Grant, G.A., Banaszak, L.J. Nat. Struct. Biol. (1995) [Pubmed]
  2. Molecular and biochemical characterization of D-phosphoglycerate dehydrogenase from Entamoeba histolytica. A unique enteric protozoan parasite that possesses both phosphorylated and nonphosphorylated serine metabolic pathways. Ali, V., Hashimoto, T., Shigeta, Y., Nozaki, T. Eur. J. Biochem. (2004) [Pubmed]
  3. Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers. Grant, G.A., Xu, X.L., Hu, Z. J. Biol. Chem. (2004) [Pubmed]
  4. The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase. Grant, G.A., Kim, S.J., Xu, X.L., Hu, Z. J. Biol. Chem. (1999) [Pubmed]
  5. Regulation of serine biosynthesis in Arabidopsis. Crucial role of plastidic 3-phosphoglycerate dehydrogenase in non-photosynthetic tissues. Ho, C.L., Noji, M., Saito, M., Saito, K. J. Biol. Chem. (1999) [Pubmed]
  6. Regulation of phosphoglycerate dehydrogenase levels and effect on serine synthesis in Escherichia coli K-12. McKitrick, J.C., Pizer, L.I. J. Bacteriol. (1980) [Pubmed]
  7. De-regulation of D-3-phosphoglycerate dehydrogenase by domain removal. Bell, J.K., Pease, P.J., Bell, J.E., Grant, G.A., Banaszak, L.J. Eur. J. Biochem. (2002) [Pubmed]
  8. The nucleotide sequence of the serA gene of Escherichia coli and the amino acid sequence of the encoded protein, D-3-phosphoglycerate dehydrogenase. Tobey, K.L., Grant, G.A. J. Biol. Chem. (1986) [Pubmed]
  9. Transient kinetic studies on the allosteric transition of phosphoglycerate dehydrogenase. Dubrow, R., Pizer, L.I. J. Biol. Chem. (1977) [Pubmed]
  10. Isolation, characterization and sequence analysis of a full-length cDNA clone encoding NADH-dependent hydroxypyruvate reductase from cucumber. Greenler, J.M., Sloan, J.S., Schwartz, B.W., Becker, W.M. Plant Mol. Biol. (1989) [Pubmed]
  11. The mechanism of end product inhibition of serine biosynthesis. V. Mechanism of serim inhibition of phosphoglycerate dehydrogenases. Winicov, I. J. Biol. Chem. (1975) [Pubmed]
  12. Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase. Thompson, J.R., Bell, J.K., Bratt, J., Grant, G.A., Banaszak, L.J. Biochemistry (2005) [Pubmed]
 
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