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Literature summary for 2.3.3.9 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
Search for more literature for 2.3.3.9

General Stability

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

Inhibitors

Inhibitors Comment Organism Structure
fluoroacetate
-
 Zea mays
glycolate
-
 Zea mays
pyruvate
-
 Zea mays

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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