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Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.9 0.0228
-
acetyl-CoA
-
Zea mays
2.3.3.9 0.098
-
glyoxylate
-
Zea mays

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.3.9 22000
-
8 * 22000, SDS-PAGE Zea mays
2.3.3.9 510000
-
gel filtration Zea mays

Organism

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

Posttranslational Modification

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.3.9
-
Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.3.9 scutellum
-
Zea mays
-

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 additional information
-
-
Zea mays
2.3.3.9 24.5
-
-
Zea mays

Storage Stability

EC Number Storage Stability Organism
2.3.3.9 -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)

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

Subunits

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.3.9 additional information
-
5.0 Zea mays
2.3.3.9 7.6
-
-
Zea mays