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Literature summary extracted from

  • Dahinden, P.; Auchli, Y.; Granjon, T.; Taralczak, M.; Wild, M.; Dimroth, P.
    Oxaloacetate decarboxylase of Vibrio cholerae: purification, characterization, and expression of the genes in Escherichia coli (2005), Arch. Microbiol., 183, 121-129.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.112 expression in Escherichia coli Vibrio cholerae

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.112 oxalate half-maximal inhibition at 0.01 mM Vibrio cholerae
4.1.1.112 oxomalonate half-maximal inhibition at 0.2 mM Vibrio cholerae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.112 Na+ dependent on Vibrio cholerae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.112 570000
-
 oxaloacetate decarboxylase OAD-2, gel filtration Vibrio cholerae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.112 additional information Vibrio cholerae after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump ?
-
 ?
4.1.1.112 additional information Vibrio cholerae O395-N1 after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.112 Vibrio cholerae Q6A1F5 oxaloacetate decarboxylase OAD-2, beta subunit; O395-N1
-
4.1.1.112 Vibrio cholerae Q6A1F6 oxaloacetate decarboxylase OAD-2, alpha subunit; O395-N1
-
4.1.1.112 Vibrio cholerae Q6A1F7 oxaloacetate decarboxylase OAD-2, gamma subunit; O395-N1
-
4.1.1.112 Vibrio cholerae Q6A1G0 oxaloacetate decarboxylase OAD-1, gamma subunit; O395-N1
-
4.1.1.112 Vibrio cholerae Q9KUH0 oxaloacetate decarboxylase OAD-1, beta subunit; O395-N1
-
4.1.1.112 Vibrio cholerae Q9KUH1 oxaloacetate decarboxylase OAD-1, alpha subunit; O395-N1
-
4.1.1.112 Vibrio cholerae O395-N1 Q6A1F5 oxaloacetate decarboxylase OAD-2, beta subunit; O395-N1
-
4.1.1.112 Vibrio cholerae O395-N1 Q6A1F6 oxaloacetate decarboxylase OAD-2, alpha subunit; O395-N1
-
4.1.1.112 Vibrio cholerae O395-N1 Q6A1F7 oxaloacetate decarboxylase OAD-2, gamma subunit; O395-N1
-
4.1.1.112 Vibrio cholerae O395-N1 Q6A1G0 oxaloacetate decarboxylase OAD-1, gamma subunit; O395-N1
-
4.1.1.112 Vibrio cholerae O395-N1 Q9KUH0 oxaloacetate decarboxylase OAD-1, beta subunit; O395-N1
-
4.1.1.112 Vibrio cholerae O395-N1 Q9KUH1 oxaloacetate decarboxylase OAD-1, alpha subunit; O395-N1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.112 enzyme from Vibrio cholerae and heterologously expressed enzyme Vibrio cholerae

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.1.1.112 heterologously expressed oxaloacetate decarboxylase OAD-2 Vibrio cholerae

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.1.1.112 culture condition:anaerobically-grown cell upon anaerobic growth of Vibrio cholerae on citrate, exclusivle the oad-2 gene is expressed Vibrio cholerae
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.112 additional information
-
-
 Vibrio cholerae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.112 additional information after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump Vibrio cholerae ?
-
 ?
4.1.1.112 additional information after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump Vibrio cholerae O395-N1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.112 tetramer oxaloacetate decarboxylase OAD-2 Vibrio cholerae

Synonyms

EC Number Synonyms Comment Organism
4.1.1.112 OAD-1
-
 Vibrio cholerae
4.1.1.112 OAD-2
-
 Vibrio cholerae
4.1.1.112 oxaloacetate decarboxylase Na+ pump
-
 Vibrio cholerae
4.1.1.112 oxaloacetate decarboxylase OAD-1
-
 Vibrio cholerae
4.1.1.112 oxaloacetate decarboxylase OAD-2
-
 Vibrio cholerae