METABOLISM OF DICARBOXYLIC ACIDS IN ACETOBACTER XYLINUM
AUTOR(ES)
Benziman, Moshe
RESUMO
Benziman, Moshe (The Hebrew University of Jerusalem, Jerusalem, Israel), and A. Abeliovitz. Metabolism of dicarboxylic acids in Acetobacter xylinum. J. Bacteriol. 87:270–277. 1964.—During the oxidation of fumarate or l-malate by whole cells or extracts of Acetobacter xylinum grown on succinate, a keto acid accumulated in the medium in considerable amounts. This acid was identified as oxaloacetic acid (OAA). No accumulation of OAA was observed when succinate served as substrate. These phenomena could be explained by the kinetics of malate, succinate, and OAA oxidation. OAA did not inhibit malate oxidation, even when present at high concentrations. When cells were incubated with OAA or fumarate in the presence of C14O2, only the beta-carboxyl of residual OAA was found to be labeled. Evidence was obtained indicating that nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) are not directly involved in malate oxidation by cell-free extracts. The results suggest that malate oxidation in A. xylinum is irreversible, and is catalyzed by an enzyme which is not NAD- or NADP-linked.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=277003Documentos Relacionados
- Role of Phosphoenolpyruvate Carboxylation in Acetobacter xylinum
- Factors Affecting Hexose Phosphorylation in Acetobacter xylinum
- Genetic organization of the cellulose synthase operon in Acetobacter xylinum.
- OXALOACETATE DECARBOXYLATION AND OXALOACETATE-CARBON DIOXIDE EXCHANGE IN ACETOBACTER XYLINUM
- Enhancement of cellulose production by expression of sucrose synthase in Acetobacter xylinum
