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Literature summary for 2.4.1.14 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

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

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Substrates and Products (Substrate)

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