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Literature summary for 2.4.1.14 extracted from

  • Chua, T.K.; Bujnicki, J.M.; Tan, T.C.; Huynh, F.; Patel, B.K.; Sivaraman, J.
    The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode (2008), Plant Cell, 20, 1059-1072.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion technique at 25°C. Crystal structure of SPS and its complexes with the substrate D-fructose 6-phosphate and the product D-sucrose-6'-phosphate. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate D-fructose 6-phosphate and the product D-fructose 6'-phosphate bind to the A-domain of SPS. Halothermothrix orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme Halothermothrix orenii

Organism

Organism UniProt Comment Textmining
Halothermothrix orenii B8CZ51
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Synonyms

Synonyms Comment Organism
SPS
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Halothermothrix orenii