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Literature summary 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

EC Number Inhibitors Comment Organism Structure
2.3.3.12 glycolaldehyde
-
Escherichia coli
2.3.3.12 glycolate
-
Escherichia coli
2.3.3.12 Glyoxal
-
Escherichia coli

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.12 Escherichia coli
-
-
-
2.3.3.12 Escherichia coli E 26
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.3.12 partial Escherichia coli

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.3.12 4.8
-
-
Escherichia coli

Substrates and Products (Substrate)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.3.12 8.5
-
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.3.12 7 9 pH 7: about 60% of maximal activity, inactive at pH 9.5 Escherichia coli