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Literature summary extracted from

  • Wedler, F.C.; Ley, B.W.
    Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-I (1993), J. Biol. Chem., 268, 4880-4888.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.3 L-threonine
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.3 0.013
-
 L-homoserine
-
 Escherichia coli
1.1.1.3 0.073
-
 NADP+
-
 Escherichia coli
1.1.1.3 0.09
-
 NADPH
-
 Escherichia coli
1.1.1.3 0.17
-
 L-aspartate 4-semialdehyde
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.3 L-aspartate 4-semialdehyde + NAD(P)H Escherichia coli kinetic mechanism L-homoserine + NAD(P)+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.3 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.3 L-aspartate 4-semialdehyde + NAD(P)H
-
 Escherichia coli L-homoserine + NAD(P)+
-
 r
1.1.1.3 L-aspartate 4-semialdehyde + NAD(P)H kinetic mechanism Escherichia coli L-homoserine + NAD(P)+
-
 r
1.1.1.3 L-homoserine + NAD(P)+
-
 Escherichia coli L-aspartate 4-semialdehyde + NAD(P)H
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.3 NADP+
-
 Escherichia coli
1.1.1.3 NADPH
-
 Escherichia coli