BRENDA - Enzyme Database

Molecular characterization of a bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase, in Euglena gracilis

Nakazawa, M.; Minami, T.; Teramura, K.; Kumamoto, S.; Hanato, S.; Takenaka, S.; Ueda, M.; Inui, H.; Nakano, Y.; Miyatake, K.; Comp. Biochem. Physiol. B 141, 445-452 (2005)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
Commentary
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
Commentary
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
30C, pH 8.0
Euglena gracilis
2.3.3.9
0.04
-
glyoxylate
30C, pH 8.0
Euglena gracilis
4.1.3.1
0.025
-
acetyl-CoA
pH 8.0, 30C
Euglena gracilis
4.1.3.1
0.04
-
glyoxylate
pH 8.0, 30C
Euglena gracilis
4.1.3.1
7.6
-
isocitrate
pH 6.5, 30C
Euglena gracilis
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Primary Accession No. (UniProt)
Commentary
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
Commentary
Organism
2.3.3.9
-
Euglena gracilis
4.1.3.1
-
Euglena gracilis
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
2.3.3.9
5.19
-
30C, 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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.3.3.9
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis
(S)-malate + CoA
-
-
-
?
2.3.3.9
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis SM-ZK
(S)-malate + CoA
-
-
-
?
4.1.3.1
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis
malate + CoA
-
-
-
?
4.1.3.1
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis SM-ZK
malate + CoA
-
-
-
?
4.1.3.1
isocitrate
-
658479
Euglena gracilis
succinate + glyoxylate
-
-
-
?
4.1.3.1
isocitrate
-
658479
Euglena gracilis SM-ZK
succinate + glyoxylate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
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
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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
Commentary
Organism
2.3.3.9
7.5
8.5
malate synthase reaction
Euglena gracilis
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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) (protein specific)
EC Number
Commentary
Organism
2.3.3.9
-
Euglena gracilis
4.1.3.1
-
Euglena gracilis
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
30C, pH 8.0
Euglena gracilis
2.3.3.9
0.04
-
glyoxylate
30C, pH 8.0
Euglena gracilis
4.1.3.1
0.025
-
acetyl-CoA
pH 8.0, 30C
Euglena gracilis
4.1.3.1
0.04
-
glyoxylate
pH 8.0, 30C
Euglena gracilis
4.1.3.1
7.6
-
isocitrate
pH 6.5, 30C
Euglena gracilis
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.3.3.9
-
Euglena gracilis
4.1.3.1
-
Euglena gracilis
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
2.3.3.9
5.19
-
30C, 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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.3.3.9
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis
(S)-malate + CoA
-
-
-
?
2.3.3.9
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis SM-ZK
(S)-malate + CoA
-
-
-
?
4.1.3.1
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis
malate + CoA
-
-
-
?
4.1.3.1
acetyl-CoA + glyoxylate + H2O
-
658479
Euglena gracilis SM-ZK
malate + CoA
-
-
-
?
4.1.3.1
isocitrate
-
658479
Euglena gracilis
succinate + glyoxylate
-
-
-
?
4.1.3.1
isocitrate
-
658479
Euglena gracilis SM-ZK
succinate + glyoxylate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
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
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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 (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
2.3.3.9
7.5
8.5
malate synthase reaction
Euglena gracilis