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. 1980 Mar;141(3):1291-7.
doi: 10.1128/jb.141.3.1291-1297.1980.

Beta-alanine synthesis in Escherichia coli

Beta-alanine synthesis in Escherichia coli

J E Cronan Jr. J Bacteriol. 1980 Mar.

Abstract

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.

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