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. 1964 Dec;88(6):1678–1687. doi: 10.1128/jb.88.6.1678-1687.1964

OXALOACETATE DECARBOXYLATION AND OXALOACETATE-CARBON DIOXIDE EXCHANGE IN ACETOBACTER XYLINUM

Moshe Benziman 1, N Heller 1
PMCID: PMC277473  PMID: 14240957

Abstract

Benziman, Moshe (The Hebrew University of Jerusalem, Jerusalem, Israel), and N. Heller. Oxaloacetate decarboxylation and oxaloacetate-carbon dioxide exchange in Acetobacter xylinum. J. Bacteriol. 88:1678–1687. 1964.—Extracts of Acetobacter xylinum, prepared by sonic treatment, were shown to catalyze the decarboxylation of oxaloacetate (OAA) to pyruvate and CO2, and the exchange of C14-carbon dioxide into the β-carboxyl of OAA. Fractionation of the extracts with ammonium sulfate resulted in a 10-fold increase of the specific activity of the enzyme system catalyzing the CO2 exchange and OAA decarboxylation reactions. The purified preparation catalyzed the exchange of pyruvate-3-C14 into OAA. Similar pH curves with a pH optimum of 5.6 were obtained for the CO2 exchange and OAA decarboxylation reactions. Both reactions require the presence of Mn2+ or Mg2+ ions. OAA decarboxylation was more strongly inhibited than the exchange of CO2 by dialysis or metal-chelating agents. Avidin did not inhibit either reaction. Adenosine triphosphate (ATP), adenosine diphosphate (ADP), guanosine triphosphate (GTP), guanosine diphosphate (GDP), pyrophosphate, or inorganic phosphate did not promote OAA decarboxylation and the CO2-exchange reaction catalyzed by the purified preparation. The purified preparation failed to catalyze the carboxylation of phosphoenolpyruvate in the presence of GDP, ADP, or inorganic phosphate, and that of pyruvate in the presence of ATP or GTP, even when supplemented with an OAA-trapping system. A scheme for OAA decarboxylation which could account for the observed exchange reactions and for the failure to obtain net fixation of CO2 is proposed. The relation between the exchange reaction and the synthesis of cellulose from pyruvate by A. xylinum is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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