TAILIEUCHUNG - Báo cáo khoa học: Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase

AraL fromBacillus subtilisis a member of the ubiquitous haloalkanoate dehalogenase superfamily. ThearaLgene has been cloned, over-expressed in Escherichia coliand its product purified to homogeneity. The enzyme displays phosphatase activity, which is optimal at neutral pH () and 65 C. | 1FEBS Journal Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily AraL from Bacillus subtilis Lia M. Godinho and Isabel de Sa-Nogueira Centro de Recursos Microbiologicos Departamento de Ciencias da Vida Faculdade de Ciencias e Tecnologia Universidade Nova de Lisboa Quinta da Torre Caparica Portugal Keywords AraL Bacillus subtilis gene regulation HAD superfamily IIA sugar phosphatase Correspondence I. de Sa-Nogueira Departamento de Ciencias da Vida Faculdade de Ciencias e Tecnologia Universidade Nova de Lisboa Quinta da Torre 2829-516 Caparica Portugal Fax 351 21 2948530 Tel 351 21 2947852 E-mail isn@ Re-use of this article is permitted in accordance with the Terms and Conditions set out at http onlineopen OnlineOpen_Terms Received 2 October 2010 revised 1 April 2011 accepted 10 May 2011 doi AraL from Bacillus subtilis is a member of the ubiquitous haloalkanoate dehalogenase superfamily. The araL gene has been cloned over-expressed in Escherichia coli and its product purified to homogeneity. The enzyme displays phosphatase activity which is optimal at neutral pH and 65 C. Substrate screening and kinetic analysis showed AraL to have low specificity and catalytic activity towards several sugar phosphates which are metabolic intermediates of the glycolytic and pentose phosphate pathways. On the basis of substrate specificity and gene context within the arabinose metabolic operon a putative physiological role of AraL in the detoxification of accidental accumulation of phosphorylated metabolites has been proposed. The ability of AraL to catabolize several related secondary metabolites requires regulation at the genetic level. In the present study using site-directed mutagenesis we show that the production of AraL is regulated by a structure in the translation initiation region of the mRNA which most probably blocks access to the .

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