Cloning and Sequence Analysis of the estA Gene Encoding Enzyme for Producing (R)-β-Acetylmercaptoisobutyric Acid from Pseudomonas aeruginosa 1001

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The estA gene encoding the enzyme that catalyzes the production of (R)-β-acetylmercaptoisobutyric acid from (R, S)-ester from Pseudomonas aeruginasa 1001, was cloned in Escherichia coli and its nucleotide sequence was determined, revealing the presumed open reading frame encoding a polypeptide of 316 amino acid residues(948 nucleotides). The overall A + T and C + G compositions were 32.59% and 67.41%, respectively. The amino acid sequence of the estA gene product showed a significant similarity with that of the triacylglycerol lipase from Psychrobacter immobilis(38% identity), triacylglycerol lipase from Moraxella sp.(36% identity), and two forms of carboxyl esterases from Acinetobacter calcoaceticus(17% and 17% identities). The deduced amino acid sequences have a pentapeptide consensus sequence, G-X-S-X-G, having an active serine residue, and another active site, dipeptides H-G, located at 70-100 amino acids upstream of the G-X-S-X-G consensus sequence.
社団法人日本生物工学会の論文
2000-12-25