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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.3.1 acetyl-CoA more than 4fold increased enzyme activity in the presence of 150 microM acetyl-CoA Euglena gracilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.3.9
-
 Euglena gracilis
4.1.3.1
-
 Euglena gracilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.9 additional information
-
 additional information bifunctional enzyme has specific catalytic features. Isocitrate lyase activity is increased by acetyl-CoA Euglena gracilis
2.3.3.9 0.025
-
 acetyl-CoA 30°C, pH 8.0 Euglena gracilis
2.3.3.9 0.04
-
 glyoxylate 30°C, pH 8.0 Euglena gracilis
4.1.3.1 0.025
-
 acetyl-CoA pH 8.0, 30°C Euglena gracilis
4.1.3.1 0.04
-
 glyoxylate pH 8.0, 30°C Euglena gracilis
4.1.3.1 7.6
-
 isocitrate pH 6.5, 30°C Euglena gracilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.3.9 110000
-
 4 * 110000, SDS-PAGE Euglena gracilis
2.3.3.9 420000
-
 gel filtration Euglena gracilis
4.1.3.1 110000
-
 4 * 110000, SDS-PAGE Euglena gracilis
4.1.3.1 420000
-
 gel filtration Euglena gracilis

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.9 Euglena gracilis Q8LPA6 bifunctional malate synthase/isocitrate lyase, induced by growth on ethanol
-
4.1.3.1 Euglena gracilis Q8LPA6 SM-ZK
-
4.1.3.1 Euglena gracilis SM-ZK Q8LPA6 SM-ZK
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.3.9
-
 Euglena gracilis
4.1.3.1
-
 Euglena gracilis

Source Tissue

EC Number Source Tissue Comment Organism Textmining

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 5.19
-
 30°C, pH 8.0 Euglena gracilis
4.1.3.1 0.636
-
 isocitrate lyase activity Euglena gracilis
4.1.3.1 5.19
-
 malate synthase activity Euglena gracilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.9 acetyl-CoA + glyoxylate + H2O
-
 Euglena gracilis (S)-malate + CoA
-
 ?
2.3.3.9 acetyl-CoA + glyoxylate + H2O
-
 Euglena gracilis SM-ZK (S)-malate + CoA
-
 ?
4.1.3.1 acetyl-CoA + glyoxylate + H2O
-
 Euglena gracilis malate + CoA
-
 ?
4.1.3.1 acetyl-CoA + glyoxylate + H2O
-
 Euglena gracilis SM-ZK malate + CoA
-
 ?
4.1.3.1 isocitrate
-
 Euglena gracilis succinate + glyoxylate
-
 ?
4.1.3.1 isocitrate
-
 Euglena gracilis SM-ZK succinate + glyoxylate
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
4.1.3.1 EgGCE bifunctional enzyme: isocitrate lyase and malate synthase Euglena gracilis
4.1.3.1 ICL
-
 Euglena gracilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.3.1 6.5
-
 isocitrate lyase Euglena gracilis
4.1.3.1 7.5 8.5 malate synthase Euglena gracilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.3.9 7.5 8.5 malate synthase reaction Euglena gracilis