A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity
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چکیده
منابع مشابه
A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity.
The phosphoenolpyruvate carboxykinase in Escherichia coli (encoded by pck) catalyzes the conversion from oxaloacetate (OAA) to phosphoenolpyruvate under gluconeogenic conditions. We report here the characterization of two mutant alleles, pck-51 and pck-53, both of which are point mutations leading to single amino acid changes (D to N at position 268 and G to S at position 284, respectively). Pc...
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Phosphoenolpyruvate and oxaloacetate are key intermediates at the junction between catabolism and biosynthesis. Alteration of carbon flow at these branch points will affect the growth yield and the formation of products. We attempted to modulate the metabolic flow between phosphoenolpyruvate and oxaloacetate by overexpressing phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase...
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Succinate fermentation was investigated in Escherichia coli strains overexpressing Actinobacillus succinogenes phosphoenolpyruvate carboxykinase (PEPCK). In E. coli K-12, PEPCK overexpression had no effect on succinate fermentation. In contrast, in the phosphoenolpyruvate carboxylase mutant E. coli strain K-12 ppc::kan, PEPCK overexpression increased succinate production 6.5-fold.
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A total of three pyridoxyl-peptides were isolated from the inducible argmine decarboxylase of Escherichia coli B following reduction with NaBH4 and proteolysis with trypsin or chymotrypsin. Sodium borohydride reduces the Schiff base formed between pyridoxal-5’-P and the e-amino group of a lysyl residue of the protein. The sequence analysis of the three peptides is consistent with a unique pyrid...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1995
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.177.6.1620-1623.1995