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Query: UMLS:C0519030 (Klebsiella)
21,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The pathways of the utilization of dicarboxylic amino acids and their amides in 55 Klebsiella strains have been studied. These organisms have been found to be capable of carboxylating glutaminic acid with the subsequent utilization of the product of this reaction, gamma-amino butyric acid, by reamidization with alpha-glutaric acid. Aspartate decarboxylase with low activity has been detected only in a small number of strains. Most of the strains have been shown to be capable of deamidizating equally asparaginic and glutaminic acids. The presence of active asparaginase and glutaminase has been detected in a considerable number of these strains. Microorganisms of the genus Klebsiella have low asparagine synthetase and glutamine synthetase activity. Aspartate aminotransferase has been found to occur twice as frequently as alanine aminotransferase, both having the same level of activity.
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PMID:[Metabolism of dicarboxylic amino acids and their amides in bacteria of the genus Klebsiella]. 711 27

The oxygen-sensitive 4-hydroxybenzoate decarboxylase (4OHB-DC) activity from a phenol-carboxylating coculture, consisting of Clostridium-like strain 6 and an unidentified strain 7, was studied. Assays done with cell extracts showed that the optimal pH was 5.0-6.5 and the Km was 5.4 mM. The activity decreased by 50% in the presence of 5 mM EDTA, and it was restored and even enhanced by the addition of Mg++, Mn++, Zn++, or Ca++. After purification, the molecular mass of the enzyme was estimated as 420 kDa by gel chromatography, and as 119 kDa by SDS-PAGE, suggesting a homotetrameric structure. Its pI was 5.6. The N-terminal amino acid sequence showed 95% and 76% homology with the pyruvate-flavodoxin oxidoreductase (nifJ gene product) from Enterobacter agglomerans and Klebsiella pneumoniae, respectively. The purified enzyme also slowly catalyzed the reverse reaction, that is the phenol carboxylation. These characteristics suggest that this enzyme is different from other known decarboxylases. This includes the 4OHB-DC from Clostridium hydroxybenzoicum, which is the only one that had been purified before.
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PMID:Purification and characterization of a 4-hydroxybenzoate decarboxylase from an anaerobic coculture. 1100 47