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Literature summary extracted from

  • Goh, L.L.; Loke, P.; Sim, T.S.
    Replacement of arginine-171 and aspartate-453 in Streptomyces coelicolor malate synthase A by site-directed mutagenesis inactivates the enzyme (2001), Appl. Microbiol. Biotechnol., 57, 363-367.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.3.9 D453A 0.06% of wild-type activity Streptomyces coelicolor
2.3.3.9 R171L 0.2% of wild-type activity, reduced expression at room temperature, expression of soluble protein at 15°C Streptomyces coelicolor

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.3.9 86000
-
 x * 86000, GST-enzyme fusion protein, SDS-PAGE Streptomyces coelicolor

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.9 Streptomyces coelicolor Q9RKU9 expression in Escherichia coli
-
2.3.3.9 Streptomyces coelicolor A3(2) Q9RKU9 expression in Escherichia coli
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.3.9 15.6
-
 mutant D453A, pH 7.9 Streptomyces coelicolor
2.3.3.9 44.2
-
 mutant R171L, pH 7.9 Streptomyces coelicolor
2.3.3.9 25090
-
 wild-type, pH 7.9 Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.9 acetyl-CoA + glyoxylate + H2O
-
 Streptomyces coelicolor (S)-malate + CoA
-
 ?
2.3.3.9 acetyl-CoA + glyoxylate + H2O
-
 Streptomyces coelicolor A3(2) (S)-malate + CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.3.9 ? x * 86000, GST-enzyme fusion protein, SDS-PAGE Streptomyces coelicolor