TAILIEUCHUNG - Báo cáo khoa học: Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation

Escherichia coliphosphotransacetylase (Pta) catalyzes the reversible inter-conversion of acetyl-CoA and acetyl phosphate. Both compounds are critical in E. colimetabolism, and acetyl phosphate is also involved in the regulation of certain signal transduction pathways. Along with acetate kinase, Pta plays an important role in acetate production when E. | ỊFEBS Journal Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation Valeria Alina Campos-Bermudez Federico Pablo Bologna Carlos Santiago Andreo and Maria Fabiana Drincovich Centro de Estudios Fotosinteticos y Bioquimicos CEFOBI Universidad Nacionalde Rosario Argentina Keywords acetyl-phosphate activity regulation Escherichia coli phosphotransacetylase protein domain Correspondence M. F. Drincovich Suipacha 531 2000 Rosario Argentina Fax 54 341 4370044 Tel 54 341 4371955 E-mail drincovich@ Received 15 January 2010 revised 11 February 2010 accepted 12 February 2010 doi Escherichia coli phosphotransacetylase Pta catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. Both compounds are critical in E. coli metabolism and acetyl phosphate is also involved in the regulation of certain signal transduction pathways. Along with acetate kinase Pta plays an important role in acetate production when E. coli grows on rich medium alternatively it is involved in acetate utilization at high acetate concentrations. E. coli Pta is composed of three different domains but only the C-terminal one called PTA_PTB is specific for all Ptas. In the present work the characterization of E. coli Pta and deletions from the N-terminal region were performed. E. coli Pta acetyl phosphate-forming and acetyl phosphate-consuming reactions display different maximum activities and are differentially regulated by pyruvate and phosphoenolpyruvate. These compounds activate acetyl phosphate production but inhibit acetyl-CoA production thus playing a critical role in defining the rates of the two Pta reactions. The characterization of three truncated Ptas which all display Pta activity indicates that the substrate-binding site is located at the C-terminal PTA_PTB domain. However the N-terminal P-loop NTPase domain is involved in expression of .

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