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Literature summary for 2.3.3.12 extracted from

  • Imai, K.; Reeves, H.C.; Ajl, S.J.
    n-Propylmalate synthetase (1963), J. Biol. Chem., 238, 3193-3198.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
glycolaldehyde
-
Escherichia coli
glycolate
-
Escherichia coli
Glyoxal
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ accelerates, optimal concentration: 0.0032 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli E 26
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Escherichia coli

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:pentanoate-grown cell
-
Escherichia coli
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.8
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pentanoyl-CoA + glyoxylate + H2O i.e. valeroyl-CoA Escherichia coli 3-propylmalate + CoA
-
?
pentanoyl-CoA + glyoxylate + H2O i.e. valeroyl-CoA Escherichia coli E 26 3-propylmalate + CoA
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7 9 pH 7: about 60% of maximal activity, inactive at pH 9.5 Escherichia coli