Beta-alanine synthesis in Escherichia coli.

AUTOR(ES)

Cronan, J E

RESUMO

The enzyme, aspartate 1-decarboxylase (L-aspartate 1-carboxy-lyase; EC 4.1.1.15), that catalyzes the reaction aspartate leads to beta-alanine + CO2 was found in extracts of Escherichia coli. panD mutants of E. coli are defective in beta-alanine biosynthesis and lack aspartate 1-decarboxylase. Therefore, the enzyme functions in the biosynthesis of the beta-alanine moiety of pantothenate. The genetic lesion in these mutants is closely linked to the other pantothenate (pan) loci of E. coli K-12.

Documentos Relacionados

• beta-Alanine auxotrophy associated with dfp, a locus affecting DNA synthesis in Escherichia coli.
• Cloning and expression of a cDNA encoding the transporter of taurine and beta-alanine in mouse brain.
• Deposition of Labeled Beta-Alanine in Ebony and Non-Ebony DROSOPHILA MELANOGASTER with Notes on Other Amino Acids
• Beta-Alanine Protection of Yeast Growth Against the Inhibitory Action of Several Chlorinated Aliphatic Acid Herbicides. 1
• Demonstration of H+- and Na+-coupled co-transport of beta-alanine by luminal membrane vesicles of rabbit proximal tubule.