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Literature summary extracted from

  • Beeckmans, S.; Khan, A.S.; Kanarek, L.; Van Driessche, E.
    Ligand binding on to maize (Zea mays) malate synthase: a structural study (1994), Biochem. J., 303, 413-421.
No PubMed abstract available

General Stability

EC Number General Stability Organism
2.3.3.9 limited proteolysis with trypsin results in cleavage of malate synthase into two framents of respectively 45000 Da and 19000 Da Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.3.9 fluoroacetate
-
 Zea mays
2.3.3.9 glycolate
-
 Zea mays
2.3.3.9 pyruvate
-
 Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.9 0.02
-
 acetyl-CoA
-
 Zea mays
2.3.3.9 0.104
-
 glyoxylate
-
 Zea mays

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.3.9 Mg2+ required Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.9 Zea mays
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.3.9 acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA compulsory-order mechanism, glyoxylate being the first-binding substrate, glyoxylate triggers a conformational change in the enzyme and as a consequence, the correctly shaped binding site for acetyl-CoA is created Zea mays
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.9 glyoxylate + acetyl-CoA + H2O
-
 Zea mays (S)-malate + CoA
-
 ?