title: Cloning and sequence analysis of the estA gene encoding enzyme for producing (R)-beta-acetylmercaptoisobutyric acid from Pseudomonas aeruginosa 1001.
abstract: The estA gene encoding the enzyme that catalyzes the production of (R)-beta-acetylmercaptoisobutyric acid from (R,S)-ester from Pseudomonas aeruginosa 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.
authors.affiliation: Applied Microbiology Research Division, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon 305-600, Korea.
authors.forename: J
authors.initials: J
authors.lastname: Lee
authors.forename: G
authors.initials: G
authors.lastname: Boyapati
authors.forename: K
authors.initials: K
authors.lastname: Song
authors.forename: S
authors.initials: S
authors.lastname: Rhee
authors.forename: C
authors.initials: C
authors.lastname: Kim