Sanchez_2012_Microbiol.Res_167_317

Reference

Title : A Pseudomonas aeruginosa PAO1 acetylcholinesterase is encoded by the PA4921 gene and belongs to the SGNH hydrolase family - Sanchez_2012_Microbiol.Res_167_317
Author(s) : Sanchez DG , Otero LH , Hernandez CM , Serra AL , Encarnacion S , Domenech CE , Lisa AT
Ref : Microbiol Res , 167 :317 , 2012
Abstract : Through the use of molecular and biochemical experiments and bioinformatic tools, this work demonstrates that the PA4921 gene of the Pseudomonas aeruginosa PAO1 genome is a gene responsible for cholinesterase (ChoE) activity. Similar to the acetylcholinesterase (AchE) of Zea mays, this ChoE belongs to the SGNH hydrolase family. In mature ChoE, i.e., without a signal peptide, (18)Ser, (78)Gly, (127)N, and (268)H are conserved aminoacyl residues. Acetylthiocholine (ATC) and propionylthiocholine (PTC) are substrates of this enzyme, but butyrylcholine is an inhibitor. The enzyme also catalyzes the hydrolysis of the artificial esters p-nitrophenyl propionate (pNPP) and p-nitrophenyl butyrate (pNPB) but with lower catalytic efficiency with respect to ATC or PTC. The second difference is that pNPP and pNPB did not produce inhibition at high substrate concentrations, as occurred with ATC and PTC. These differences plus preliminary biochemical and kinetic studies with alkylammonium compounds led us to propose that this enzyme is an acetylcholinesterase (AchE) or propionylcholinesterase. Studies performed with the purified recombinant enzyme indicated that the substrate saturation curves and the catalytic mechanism are similar to those properties described for mammalian AchEs. Therefore, the results of this work suggest that the P. aeruginosa ChoE is an AchE that may also be found in Pseudomonas fluorescens.
ESTHER : Sanchez_2012_Microbiol.Res_167_317
PubMedSearch : Sanchez_2012_Microbiol.Res_167_317
PubMedID: 22192836

Related information

Citations formats

Sanchez DG, Otero LH, Hernandez CM, Serra AL, Encarnacion S, Domenech CE, Lisa AT (2012)
A Pseudomonas aeruginosa PAO1 acetylcholinesterase is encoded by the PA4921 gene and belongs to the SGNH hydrolase family
Microbiol Res 167 :317

Sanchez DG, Otero LH, Hernandez CM, Serra AL, Encarnacion S, Domenech CE, Lisa AT (2012)
Microbiol Res 167 :317

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    [id] => 218221
    [paper] => Sanchez_2012_Microbiol.Res_167_317
    [author] => Sanchez DG || Otero LH || Hernandez CM || Serra AL || Encarnacion S || Domenech CE || Lisa AT
    [year] => 2012
    [title] => A Pseudomonas aeruginosa PAO1 acetylcholinesterase is encoded by the PA4921 gene and belongs to the SGNH hydrolase family
    [journal] => Microbiol Res
    [volume] => 167
    [page] => 317
    [medline] => 22192836
    [abstract] => Sanchez_2012_Microbiol.Res_167_317
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    [comment] => This enzyme Q9HUP2_PSEAE in UniProt) is not an alpha\/beta hydrolase. It belongs to the clan SGNH_hydrolase (CL0264) in Pfam. It is unrelated to the enzyme described by Rochu et al.<\/A> in Pseudomonas fluorescens
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            [id] => 172909
            [longtext] => Sanchez_2012_Microbiol.Res_167_317
            [content] => Through the use of molecular and biochemical experiments and bioinformatic tools, this work demonstrates that the PA4921 gene of the Pseudomonas aeruginosa PAO1 genome is a gene responsible for cholinesterase (ChoE) activity. Similar to the acetylcholinesterase (AchE) of Zea mays, this ChoE belongs to the SGNH hydrolase family. In mature ChoE, i.e., without a signal peptide, (18)Ser, (78)Gly, (127)N, and (268)H are conserved aminoacyl residues. Acetylthiocholine (ATC) and propionylthiocholine (PTC) are substrates of this enzyme, but butyrylcholine is an inhibitor. The enzyme also catalyzes the hydrolysis of the artificial esters p-nitrophenyl propionate (pNPP) and p-nitrophenyl butyrate (pNPB) but with lower catalytic efficiency with respect to ATC or PTC. The second difference is that pNPP and pNPB did not produce inhibition at high substrate concentrations, as occurred with ATC and PTC. These differences plus preliminary biochemical and kinetic studies with alkylammonium compounds led us to propose that this enzyme is an acetylcholinesterase (AchE) or propionylcholinesterase. Studies performed with the purified recombinant enzyme indicated that the substrate saturation curves and the catalytic mechanism are similar to those properties described for mammalian AchEs. Therefore, the results of this work suggest that the P. aeruginosa ChoE is an AchE that may also be found in Pseudomonas fluorescens.
        )

)