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Literature summary for 4.1.2.5 extracted from

  • Dainty, R.H.
    Purification and properties of threonine aldolase from Clostridium pasteurianum (1970), Biochem. J., 117, 585-592.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol activity is decreased to 20% of the original by treatment with cysteine plus mercaptoethanol. Most of the loss is regained on incubation with pyridoxal 5'-phosphate Clostridium pasteurianum
cysteine activity is decreased to 20% of the original by treatment with cysteine plus mercaptoethanol. Most of the loss is regained on incubation with pyridoxal 5'-phosphate Clostridium pasteurianum
hydroxylamine 1 mM, complete inhibition Clostridium pasteurianum
Semicarbazide 1 mM, complete inhibition Clostridium pasteurianum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.42
-
L-threonine pH 7.0, 30°C Clostridium pasteurianum

Organism

Organism UniProt Comment Textmining
Clostridium pasteurianum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Clostridium pasteurianum

Storage Stability

Storage Stability Organism
0-5°C, activity slowly decreases to 50% of the original activity after 10 days Clostridium pasteurianum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threonine the enzyme is highly specific for L-threonine, no activity with D-threonine, no activity with DL-allo-threonine Clostridium pasteurianum glycine + acetaldehyde
-
r

Synonyms

Synonyms Comment Organism
L-threonine acetaldehyde-lyase
-
Clostridium pasteurianum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7
-
Clostridium pasteurianum

pH Range

pH Minimum pH Maximum Comment Organism
6 7.8 pH 6.0: about 80% of maximal activity, pH 7.8: about 80% of maximal activity Clostridium pasteurianum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Clostridium pasteurianum