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Literature summary for 2.7.2.3 extracted from

  • Bernstein, B.E.; Michels, P.A.; Hol, W.G.
    Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation (1997), Nature, 385, 275-278.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of the glycosomal enzyme lacking the C-terminal glycosome-specific 20-residue signal sequence, in Escherichia coli Trypanosoma brucei

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion method, protein solution containing 2.5 M potassium sodium phosphate, pH 8.0, X-ray diffraction structure determination and analysis Trypanosoma brucei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + 3-phospho-D-glyceroyl phosphate Trypanosoma brucei key enzyme in glycolysis ATP + 3-phospho-D-glycerate
-
r

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from Escherichia coli, to homogeneity Trypanosoma brucei

Reaction

Reaction Comment Organism Reaction ID
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate mechanism, substrate-induced effects combine synergistically to induce major conformational changes of the active site to catalytic status Trypanosoma brucei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + 3-phospho-D-glyceroyl phosphate key enzyme in glycolysis Trypanosoma brucei ATP + 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
-
Trypanosoma brucei ADP + 1,3-diphosphoglycerate
-
r

Subunits

Subunits Comment Organism
More ternary structure Trypanosoma brucei

Cofactor

Cofactor Comment Organism Structure
ADP
-
Trypanosoma brucei
ATP required as phosphate donor Trypanosoma brucei