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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


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