[Cloning and sequencing of the gene encoding esterase estA from Ralstonia eutropha CH34].
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.
Song
S
S
Biology Institute, Hebei Academy of Sciences, Shijazhuang 050051, China.
Steinbüchel
A
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D020118:Cupriavidus necator / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D004950:Esterases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D001426:Bacterial Proteins; D004950:Esterases