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Literature summary extracted from

  • Ramos, C.; Delgado, M.A.; Calderon, I.L.
    Inhibition by different amino acids of the aspartate kinase and the homoserine kinase of the yeast Saccharomyces cerevisiae (1991), FEBS Lett., 278, 123-126.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.39 L-homoserine
-
 Saccharomyces cerevisiae
2.7.1.39 L-Thr half-maximal inhibition at 10 mM Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.39 0.25
-
 L-homoserine pH 7.5, 30°C Saccharomyces cerevisiae
2.7.1.39 0.6
-
 ATP pH 7.5, 30°C Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.39 ATP + L-homoserine Saccharomyces cerevisiae the enzyme plays an important role in the regulation of the threonine biosynthesis ADP + O-phospho-L-homoserine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.39 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.39 ATP + L-homoserine
-
 Saccharomyces cerevisiae ADP + O-phospho-L-homoserine
-
 ?
2.7.1.39 ATP + L-homoserine the enzyme plays an important role in the regulation of the threonine biosynthesis Saccharomyces cerevisiae ADP + O-phospho-L-homoserine
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.39 2
-
 L-homoserine pH 7.5, 30°C Saccharomyces cerevisiae