Beta-alanine synthesis in Escherichia coli.
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.
D000409:Alanine / Q000096:biosynthesis*; D001224:Aspartic Acid / Q000378:metabolism; D002262:Carboxy-Lyases / Q000378:metabolism*; D002874:Chromosome Mapping; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005796:Genes; D005968:Glutamate Decarboxylase / Q000378:metabolism*; D007700:Kinetics; D010205:Pantothenic Acid / Q000096:biosynthesis; D013379:Substrate Specificity; D014498:Uracil / Q000031:analogs & derivatives / Q000494:pharmacology; D015091:beta-Alanine / Q000096:biosynthesis*
C007419:dihydrouracil; D015091:beta-Alanine; D010205:Pantothenic Acid; D001224:Aspartic Acid; D014498:Uracil; D002262:Carboxy-Lyases; D005968:Glutamate Decarboxylase; D000409:Alanine