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Literature summary extracted from

  • Cakir, B.; Tuncel, A.; Green, A.R.; Koper, K.; Hwang, S.K.; Okita, T.W.; Kang, C.
    Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry (2015), FEBS Lett., 589, 1444-1449.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.27 expression in Escherichia coli Solanum tuberosum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.27 isothermal titration calorimetry of substrate binding properties. The wild type heterotetramer possesses two distinct types of ATP binding sites, whereas the homotetrameric large/small subunit and small/small subunit variant forms only exhibit properties of one of the two binding sites. The wild type enzyme also exhibits significantly increased affinity to ATP compared to the homotetrameric enzyme forms. No stable binding is evident for glucose-1-phosphate, in the presence or absence of ATPgammaS supporting the Theorell-Chance bi-bi reaction mechanism Solanum tuberosum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.27 0.158
-
 alpha-D-glucose 1-phosphate heterodimer of small/large subunit, presence of ATPgammaS, pH 7.4, 25°C Solanum tuberosum
2.7.7.27 0.17
-
 ATP heterodimer of small/large subunit, pH 7.4, 25°C Solanum tuberosum
2.7.7.27 0.194
-
 alpha-D-glucose 1-phosphate heterodimer of small/large subunit, pH 7.4, 25°C Solanum tuberosum
2.7.7.27 0.2
-
 ATP small subunit, pH 7.4, 25°C Solanum tuberosum

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 Solanum tuberosum Q00081 and P23509 Q00081 i.e. large subunit, P23509 i.e. small subunit
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Solanum tuberosum diphosphate + ADP-glucose
-
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