Purpose: The PBP4* is a Penicillin Binding Protein belonging to the class C of AmpH type whose function remains poorly understood. This study aimed to evaluate the biophysical and enzymatic properties of the Bacillus subtilis PBP4* to gain insights into its role in the context of bacterial cell wall recycling. Methods: To characterize the PBP4*, the full-length PBP4* and its N-terminal penicillin-binding domain have been produced in Escherichia coli and purified. Results: A comparison of biophysical properties has shown that both recombinant proteins are monomeric in solution and retain the same thermal stability. On the other hand, the D-alanine methyl esterase activity detected with the full-length PBP4* is impeded by the cleavage of the 92 amino acid C-terminal domain. The esterase activity of the full-length PBP4* strates a clear D-stereospecificity. The PBP4* is also active on B. subtilis cell walls bearing teichoic acids, compounds commonly substituted with D-alanine residues. Conclusions: Our results are in agreement with the hypothesis that PBP4* could play a role in recycling cell wall components, as previously suggested.
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机译:Structure Determination and Mechanistic Insights of: I.Cyanobacteriochrome NpR6012g4 Light Sensor Protein in Phototaxis II.Retinal Degeneration 3 (RD3) Protein in Vision III.Ryanodine Receptor 2 (RyR2) Regulation by Calmodulin (CaM) in Cardiac Function =结构测定和机理洞悉:I.趋光性中的蓝细菌色素NpR6012g4光敏蛋白 II.视觉作用中的视网膜退化蛋白3 III.心脏功能中的钙调蛋白调控兰诺定受体2
机译:芽孢杆菌,蜡状芽孢杆菌,球形芽孢杆菌和枯草芽孢杆菌Bioacumulaçãodecobre,zinco,cádmioe chumbo por Bacillus sp。,Bacillus cereus,Bacillus sphaericus e Bacillus subtilis对铜,锌,镉和铅的生物累积