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Literature summary for 2.7.2.3 extracted from

  • Varga, A.; Szabo, J.; Flachner, B.; Gugolya, Z.; Vonderviszt, F.; Zavodszky, P.; Vas, M.
    Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase (2009), FEBS Lett., 583, 3660-3664.
    View publication on PubMed
Search for more literature for 2.7.2.3

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed in the Escherichia coli BL21-CodonPlus (DE3)-RIL Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information deleted T393, substrate binding abilities are hardly changed, but the substrate antagonism, characteristics of the wild-type enzyme, is completely abolished Homo sapiens
N336A substrate binding abilities are hardly changed, but the substrate antagonism, characteristics of the wild-type enzyme, is restricted Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by sonication Homo sapiens

Storage Stability

Storage Stability Organism
-80°C, 50 mM Tris-HCl, 1 mM EDTA buffer, pH 7.5, 1 mM 2-mercaptoethanol Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Mg-ADP or Mg-beta,gamma-imido-adenosine 5'-triphosphate substitute the substrate Mg-ATP in the ternary complexes, they cannot react with 3-phospho-D-glyceroyl phosphate. Domain closure and substrate antagonism are closely related phenomena for PGK. Conformational rearrangements in the hinge generated by binding of both substrates provide the main driving force for domain closure overcoming the slightly unfavourable contact interactions between the domains Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
3-phosphoglycerate kinase
-
 Homo sapiens
PGK
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
additional information in the presence of either beta,gamma-imido-adenosine 5'-triphosphate or ADP binding of 3-phospho-D-glycerate is weakened and the contribution of the entropy-factor to its binding is increased relative to the enthalpy factor Homo sapiens