Sequence and structure of yeast phosphoglycerate kinase.
The structure of yeast phosphoglycerate kinase has been determined with data obtained from amino acid sequence, nucleotide sequence, and X-ray crystallographic studies. The substrate binding sites, as deduced from electron density maps, are compatible with known substrate specificity and the stereochemical requirements for the enzymic reaction. A carboxyl-imidazole interaction appears to be involved in controlling the transition between the open and closed forms of the enzyme.
D000595:Amino Acid Sequence; D008958:Models, Molecular; D010735:Phosphoglycerate Kinase / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity; D014961:X-Ray Diffraction
D010735:Phosphoglycerate Kinase