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Literature summary for 2.3.3.9 extracted from

  • Nakazawa, M.; Minami, T.; Teramura, K.; Kumamoto, S.; Hanato, S.; Takenaka, S.; Ueda, M.; Inui, H.; Nakano, Y.; Miyatake, K.
    Molecular characterization of a bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase, in Euglena gracilis (2005), Comp. Biochem. Physiol. B, 141, 445-452.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Euglena gracilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information bifunctional enzyme has specific catalytic features. Isocitrate lyase activity is increased by acetyl-CoA Euglena gracilis
0.025
-
acetyl-CoA 30°C, pH 8.0 Euglena gracilis
0.04
-
glyoxylate 30°C, pH 8.0 Euglena gracilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
4 * 110000, SDS-PAGE Euglena gracilis
420000
-
gel filtration Euglena gracilis

Organism

Organism UniProt Comment Textmining
Euglena gracilis Q8LPA6 bifunctional malate synthase/isocitrate lyase, induced by growth on ethanol
-

Purification (Commentary)

Purification (Comment) Organism
-
Euglena gracilis

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.19
-
30°C, pH 8.0 Euglena gracilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + glyoxylate + H2O
-
Euglena gracilis (S)-malate + CoA
-
?
acetyl-CoA + glyoxylate + H2O
-
Euglena gracilis SM-ZK (S)-malate + CoA
-
?

Subunits

Subunits Comment Organism
More enzyme consists of N-terminal malate synthase domain fused to C-terminal isocitrate lyase domain Euglena gracilis
tetramer 4 * 110000, SDS-PAGE Euglena gracilis

pH Range

pH Minimum pH Maximum Comment Organism
7.5 8.5 malate synthase reaction Euglena gracilis