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Literature summary for 2.3.3.9 extracted from

  • Khan, A.S.; Van Driessche, E.; Kanarek, L.; Beeckmans, S.
    Purification of the glyoxylate cycle enzyme malate synthase from maize (Zea mays L.) and characterization of a proteolytic fragment (1993), Protein Expr. Purif., 4, 519-528.
    View publication on PubMed
Search for more literature for 2.3.3.9

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0228
-
 acetyl-CoA
-
 Zea mays
0.098
-
 glyoxylate
-
 Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22000
-
 8 * 22000, SDS-PAGE Zea mays
510000
-
 gel filtration Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no modification contains no covalent linked carbohydrate residues Zea mays

Purification (Commentary)

Purification (Comment) Organism
-
 Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
scutellum
-
 Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Zea mays
24.5
-
-
 Zea mays

Storage Stability

Storage Stability Organism
-70°C, 200 mM Hepes buffer, containing 6 mM MgCl2, 2 mM 2-mercaptoethanol, pH 7.6, stable for several months Zea mays

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
octamer 8 * 22000, SDS-PAGE Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 5.0 Zea mays
7.6
-
-
 Zea mays