2.3.3.9: malate synthase
This is an abbreviated version!
For detailed information about malate synthase, go to the full flat file.
Word Map on EC 2.3.3.9
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2.3.3.9
-
isocitrate
-
peroxisomal
-
icl
-
glyoxysomal
-
catalase
-
citrate
-
tricarboxylic
-
tuberculosis
-
shunt
-
cotyledons
-
seedling
-
microbodies
-
cucumber
-
gluconeogenesis
-
beta-oxidation
-
4.1.3.1
-
anaplerotic
-
fumarase
-
thiolase
-
cucumis
-
phosphotransacetylase
-
trosy
-
hydroxypyruvate
-
acetate-grown
-
agriculture
-
3-ketoacyl-coa
-
pumpkin
- 2.3.3.9
- isocitrate
- peroxisomal
- icl
- glyoxysomal
- catalase
- citrate
-
tricarboxylic
- tuberculosis
-
shunt
- cotyledons
- seedling
- microbodies
- cucumber
-
gluconeogenesis
-
beta-oxidation
-
4.1.3.1
-
anaplerotic
- fumarase
-
thiolase
-
cucumis
- phosphotransacetylase
-
trosy
- hydroxypyruvate
-
acetate-grown
- agriculture
- 3-ketoacyl-coa
-
pumpkin
Reaction
Synonyms
EC 4.1.3.2, GCE, GCE(13-573), glcB, glyoxylate cycle enzyme, glyoxylate transacetase, glyoxylic transacetase, L-malate glyoxylate-lyase (CoA-acetylating), malate synthase, malate synthase 1, malate synthase A, malate synthase G, malate synthase H, malate synthetase, malic synthetase, malic-condensing enzyme, MLS, MSA, MSG, MSH, SSO1334
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Metals Ions
Metals Ions on EC 2.3.3.9 - malate synthase
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Co2+
Mg2+
Mn2+
additional information
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Co2+, Fe2+, Ca2+, Ba2+, Ni2+, Cd2+, Zn2+, Cu2+, Hg2+ are not able to support the activity of enzyme
Mg2+
absolute requirement for divalent cation, maximal activity with 40 mM Mg2+
Mg2+
-
enzyme-substrate complex with glyoxylate and Mg2+, Glu427 and Asp455 bind the magnesium ion
Mg2+
enzyme catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to form malate in a magnesium-dependent manner
Mg2+
-
absolute requirement for divalent metal ion, best fulfilled by Mg2+
Mg2+
-
absolute requirement for divalent cation, maximal activity with 5 mM Mg2+
Mg2+
-
binding of acetyl-CoA to the synthase is independent of Mg2+ but that of glyoxylate is strictly dependent on the presence of Mg2+
Mg2+
-
causes no structurel effects, suggesting the metal ion to be involved in enzymatic catalysis rather than structural alternations