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Literature summary for 4.3.1.17 extracted from

  • Newman, E.B.; Walker, C.; Ziegler-Skylakis, K.
    A possible mechanism for the in vitro activation of L-serine deaminase activity in Escherichia coli K12 (1990), Biochem. Cell Biol., 68, 723-728.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information the enzyme is inactive in crude extract and can be activated with iron and dithiothreitol. The activation requires oxygen, and is inhibited by free radical scavengers and by diethylenentriamine pentaacetic acid, which prevents Fe cycling Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
D-His
-
Escherichia coli
imidazole
-
Escherichia coli
L-His
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
K12
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
Escherichia coli pyruvate + NH3
-
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