Cloning and sequence analysis of the estA gene encoding enzyme for producing (R)-β-Acetylmercaptoisobutyric acid from Pseudomonas aeruginosa 1001

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Title
Cloning and sequence analysis of the estA gene encoding enzyme for producing (R)-β-Acetylmercaptoisobutyric acid from Pseudomonas aeruginosa 1001
Author(s)
Je Hyuk Lee; Gokul Boyapati; Ki Bang Song; Sang Ki Rhee; Chul Ho Kim
Bibliographic Citation
Journal of Bioscience and Bioengineering, vol. 90, no. 6, pp. 684-687
Publication Year
2000
Abstract
The estA gene encoding the enzyme that catalyzes the production of (R)-β-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.
Keyword
(R)-β-acetylmercaptoisobutyric acidEsterase geneG-X-S-X-GNucleotide sequencePseudomonas aeruginosa
ISSN
1389-1723
Publisher
Soc Bioscience Bioengineering Japan
DOI
http://dx.doi.org/10.1016/S1389-1723(00)90019-7
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
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