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Literature summary for 2.3.3.9 extracted from

  • Howard, B.R.; Endrizzi, J.A.; Remington, S.J.
    Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 ANG resolution: Mechanistic implications (2000), Biochemistry, 39, 3156-3168.
    View publication on PubMed
Search for more literature for 2.3.3.9

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of enzyme based on a beta8/alpha8 barrel fold Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mg2+ enzyme-substrate complex with glyoxylate and Mg2+, Glu427 and Asp455 bind the magnesium ion Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
81000
-
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glyoxylate + acetyl-CoA + H2O Escherichia coli enzyme specifically involved in glyoxalate cycle metabolism (S)-malate + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyoxylate + acetyl-CoA + H2O
-
 Escherichia coli (S)-malate + CoA
-
 ?
glyoxylate + acetyl-CoA + H2O enzyme specifically involved in glyoxalate cycle metabolism Escherichia coli (S)-malate + CoA
-
 ?