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Literature summary extracted from

  • Stoecklein, W.; Schmidt, H.L.
    Evidence for L-threonine cleavage and allo-threonine formation by different enzymes from Clostridium pasteurianum: threonine aldolase and serine hydroxymethyltransferase (1985), Biochem. J., 232, 621-622.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.5 acetaldehyde the enzymic cleavage of L-threonine stops when about 30% of the amino acid is converted to glycine and acetaldehyde. By dialysis of the incubation medium against buffer the full activity of the enzyme is restored, product inhibition Clostridium pasteurianum
4.1.2.5 glycine the enzymic cleavage of L-threonine stops when about 30% of the amino acid is converted to glycine and acetaldehyde. By dialysis of the incubation medium against buffer the full activity of the enzyme is restored, product inhibition Clostridium pasteurianum

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.5 Clostridium pasteurianum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.5 L-threonine no activity with L-allo-threonine Clostridium pasteurianum glycine + acetaldehyde
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.2.5 7
-
-
 Clostridium pasteurianum

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.5 pyridoxal 5'-phosphate
-
 Clostridium pasteurianum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.2.5 0.01
-
 glycine pH and temperature not specified in the publication Clostridium pasteurianum
4.1.2.5 0.4
-
 acetaldehyde pH and temperature not specified in the publication Clostridium pasteurianum