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Literature summary 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

Cloned(Commentary)

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.112 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

EC Number Organism UniProt Comment Textmining
4.1.1.112 Vibrio cholerae serotype O1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.112
-
Vibrio cholerae serotype O1

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.1.1.112 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

EC Number Synonyms Comment Organism
4.1.1.112 OAD
-
Vibrio cholerae serotype O1

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.112 biotin
-
Vibrio cholerae serotype O1