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Literature summary extracted from

  • Huber, S.C.; Huber, J.L.
    In vitro phosphorylation and inactivation of spinach leaf sucrose-phosphate synthase by an endogenous protein kinase (1990), Biochim. Biophys. Acta, 1091, 393-400.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.14 light active, dephosphorylated is formed in light period Spinacia oleracea

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.14 additional information preparation contains a protein kinase that can phosphorylate and therefore inactivate enzyme activity Spinacia oleracea
2.4.1.14 phosphate maximum inhibition with 1.5-2 mol phosphate per mol tetramer, maximum velocity is not affected Spinacia oleracea

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.14 UDP-alpha-D-glucose + D-fructose 6-phosphate Spinacia oleracea catalyzes the penultimate step of sucrose synthesis UDP + sucrose 6-phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.14 Spinacia oleracea
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-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.14 partial Spinacia oleracea

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.14 leaf
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Spinacia oleracea
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.14 UDP-alpha-D-glucose + D-fructose 6-phosphate
-
Spinacia oleracea UDP + sucrose 6-phosphate
-
?
2.4.1.14 UDP-alpha-D-glucose + D-fructose 6-phosphate catalyzes the penultimate step of sucrose synthesis Spinacia oleracea UDP + sucrose 6-phosphate
-
?