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Literature summary for 4.1.1.112 extracted from

  • Balsera, M.; Buey, R.M.; Li, X.D.
    Quaternary structure of the oxaloacetate decarboxylase membrane complex and mechanistic relationships to pyruvate carboxylases (2011), J. Biol. Chem., 286, 9457-9467.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.112

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta (C43) cells Vibrio cholerae serotype O1

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ subunit Oad-gamma contains a Zn(II)-bound metal Vibrio cholerae serotype O1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
530000
-
 the most prominent band at 530 kDa is likely composed of a tetrameric Oad-alpha/gamma plus a dimeric (or tetrameric) Oad-beta subunit, SDS-PAGE Vibrio cholerae serotype O1

Organism

Organism UniProt Comment Textmining
Vibrio cholerae serotype O1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Vibrio cholerae serotype O1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Oxaloacetate
-
 Vibrio cholerae serotype O1 Pyruvate + CO2
-
 ?

Subunits

Subunits Comment Organism
heterotrimer OAD contains three different subunits: Oad-alpha, a biotinylated extrinsic protein that catalyzes the alpha-ketodecarboxylation of oxaloacetate; Oad-gamma, a structural bitopic membrane protein whose cytosolic tail (named as Oad-gamma’) binds tightly to Oad-alpha, and Oad-beta, a multispan transmembrane-alpha-helical protein that constitutes the Na+-channel Vibrio cholerae serotype O1

Synonyms

Synonyms Comment Organism
OAD
-
 Vibrio cholerae serotype O1

Cofactor

Cofactor Comment Organism Structure
biotin
-
 Vibrio cholerae serotype O1