The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. Minimal functions and physiological condictions required for growth of Salmonella enterica on ethanolamine in the absence of the metabolosome. In vivo and in vitro analyses of single-amino acid variants of the Salmonella enterica phosphotransacetylase enzyme provide insights into the function of its N-terminal domain. The eutD gene of Salmonella enterica encodes a protein with phosphotransacetylase enzyme activity. Escherichia coli malic enzymes: two isoforms with substantial differences in kinetic properties, metabolic regulation and structure. The complete genome sequence of Escherichia coli K-12. Microbial metabolism of amino alcohols: purification and properties of coenzyme B12-dependent ethanolamine ammonia-lyase of Escherichia coli. Microbial metabolism of amino alcohols: control of formation and stability of partially purified ethanolamine ammonia-lyase in Escherichia coli. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. However, under certain growth conditions, they can fulfil equal roles in E. Overall, the results indicate that EcEutD and Pta, although able to catalyse the same reaction, display differential efficiency and regulation, and also differ in the induction of their expression. In this case, the expression of a phosphotransacetylase different from Pta was confirmed by activity assays. coli pta acs double-mutant strain, was complemented by either introducing EcEutD or by inducing the eut operon with ethanolamine. coli, certain divergent regions of the primary structure responsible for their unique properties can be found. When comparing EutD and Pta, both from E. coli Pta (EcPta) in catalyzing its reaction in either direction and assembles as a dimer, being differentially modulated by EcPta effectors. The enzyme is a more efficient phosphotransacetylase than E. In the present work, a detailed characterization of EutD from E. coli phosphotransacetylase (Pta) remains unclear.
This enzyme has not been characterized yet, and its relationship to the multimodular E. EutD is composed only by this domain and belongs to the ethanolamine operon. The Escherichia coli genes pta and eutD encode proteins containing the phosphate-acetyltransferase domain.