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Literature summary for 2.3.3.9 extracted from

  • Nakazawa, M.; Nishimura, M.; Inoue, K.; Ueda, M.; Inui, H.; Nakano, Y.; Miyatake, K.
    Characterization of a bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase, of Euglena gracilis (2011), J. Eukaryot. Microbiol., 58, 128-133.
    View publication on PubMed
Search for more literature for 2.3.3.9

Cloned(Commentary)

Cloned (Comment) Organism
wild type enzyme is expressed in Escherichia coli BL21(DE3) cells, mutant enzymes are expressed in Escherichia coli ArcticExpress(DE3) RP cells Euglena gracilis

Protein Variants

Protein Variants Comment Organism
D475N the glyoxylate cycle enzyme mutant completely loses malate synthase activity but retains isocitrate lyase activity Euglena gracilis
additional information the C-terminal domain of the glyoxylate cycle enzyme, when expressed alone (GCE(566-1165)), does not show any enzyme activity Euglena gracilis
R187K the glyoxylate cycle enzyme mutant completely loses malate synthase activity but retains isocitrate lyase activity Euglena gracilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.065
-
 glyoxylate wild type full-length glyoxylate cycle enzyme, at 25°C, pH not specified in the publication Euglena gracilis
0.073
-
 glyoxylate N-terminal malate synthase-active domain GCE(13-573) of glyoxylate cycle enzyme, at 25°C, pH not specified in the publication Euglena gracilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62000
-
 x * 62000, the 62000 Da N-terminal domain of glyoxylate cycle enzyme provides malate synthase activity, SDS-PAGE Euglena gracilis

Organism

Organism UniProt Comment Textmining
Euglena gracilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE Sepharose column chromatography, HisTrap HP column chromatography, and Superdex 200 pg gel filtration Euglena gracilis

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 62000, the 62000 Da N-terminal domain of glyoxylate cycle enzyme provides malate synthase activity, SDS-PAGE Euglena gracilis

Synonyms

Synonyms Comment Organism
GCE
-
 Euglena gracilis
GCE(13-573) N-terminal malate synthase-active domain of glyoxylate cycle enzyme Euglena gracilis
glyoxylate cycle enzyme bifunctional enzyme possessing malate synthase and isocitrate lyase activities Euglena gracilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
14
-
 glyoxylate N-terminal malate synthase-active domain GCE(13-573) of glyoxylate cycle enzyme, at 25°C, pH not specified in the publication Euglena gracilis
17
-
 glyoxylate wild type full-length glyoxylate cycle enzyme, at 25°C, pH not specified in the publication Euglena gracilis