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Literature summary for 7.2.4.1 extracted from

  • Di Berardino, M.; Dimroth, P.
    Aspartate 203 of the oxaloacetate decarboxylase beta-subunit catalyses both the chemical and vectorial reaction of the Na+ pump (1996), EMBO J., 15, 1842-1849.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
D149E mutation within putative membrane-spanning domains of the beta-subunit. Mutant retains oxaloacetate decarboxylase and Na+ transport activities Klebsiella pneumoniae
D149Q mutation within putative membrane-spanning domains of the beta-subunit. Mutant retains oxaloacetate decarboxylase and Na+ transport activities Klebsiella pneumoniae
D203E loss of oxaloacetate decarboxylase and Na+ transport activities, mutant retains the ability to form the carboxybiotin enzyme Klebsiella pneumoniae
D203N loss of oxaloacetate decarboxylase and Na+ transport activities, mutant retains the ability to form the carboxybiotin enzyme Klebsiella pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound beta-subunit of the oxaloacetate decarboxylase Na+ pump is responsible for the decarboxylation of carboxybiotin and the coupled translocation of Na+ ions across the membrane Klebsiella pneumoniae 16020
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Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
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-
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Reaction

Reaction Comment Organism Reaction ID
a carboxybiotinyl-[protein] + n Na+[side 1] + H+[side 2] = CO2 + a biotinyl-[protein] + n Na+[side 2] residue Asp2O3 in its dissociated form binds Na+ and promotes its translocation, while the protonated residue transfers the proton to the acid-labile carboxybiotin which initiates its decarboxylation. Na+ transport by oxaloacetate decarboxylation is accompanied by H+ transport in the opposite direction Klebsiella pneumoniae
a