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[Cloning and sequencing of the gene encoding esterase estA from Ralstonia eutropha CH34]
1Biology Institute, Hebei Academy of Sciences, Shijazhuang 050051, China.
Wei Sheng Wu Xue Bao = Acta Microbiologica Sinica
|January 30, 2003
Abstract:
An esterase-positive clone was isolated by screening a genomic library of Ralstonia eutropha CH34 constructed in Escherichia coli S17-1 with top agar containing alpha-naphtyl acetate and Fast Blue RR. A gne encoding esterase activity, estA was subcloned from this clone. Nucleotide sequencing of estA showed that it was a 825 bp open reading frame, encoding an esterase EstA, composed of 275 amino acids with a predicted molecular mass of 30,785 D. Homology analysis revealed that EstA exhibited significant amino acid similarity with the enzymes involved in the meta-cleavage pathway in the metaboleism of aromatic acid compounds.