Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.2.3 extracted from

  • Sherman, M.A.; Chen, Y.; Mas, M.T.
    An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure (1997), Protein Sci., 6, 882-891.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information construction of a deletion mutant in which the C-terminal peptide is attached to the N-terminal domain plus interdomain helix through a flexible peptide linker, thus eliminating the C-terminal domain entirely, the N-terminal domain is soluble, monomeric, compactly folded, native-like in structure, and capable of binding 3-phospho-D-glycerate with high affinity Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-phospho-D-glycerate the isolated N-terminal domain is soluble, monomeric, compactly folded, native-like in structure, and capable of binding 3-phospho-D-glycerate with high affinity Saccharomyces cerevisiae ADP + 1,3-diphosphoglycerate
-
r

Cofactor

Cofactor Comment Organism Structure
ADP
-
Saccharomyces cerevisiae
ATP required as phosphate donor Saccharomyces cerevisiae