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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference39 articles.
1. Acyl carrier protein. VIII. Studies of acyl carrier protein and coenzyme A in Eschenichia coi pantothenate or ,-alanine auxotrophs;Alberts A. W.;J. Biol. Chem.,1966
2. Recalibrated linkage map of Eswherichia coli K-12;Bachmsnn B. J.;Bacteriol. Rev.,1976
3. Boeker E. A. and E. S. Snell. 1972. Amino acid decarboxylases p. 217-263. In P. Boyer (ed.) The enzymes vol. VI Academic Pres Inc. New York.
4. The amino acid pool in Ewcherichia coli;Britten R. G.;Bacteriol. Rev.,1962
5. The metabolism of pantothenic acid;Brown G. M.;J. Biol. Chem.,1959
Cited by
117 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献