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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

Authors 

Je Hyuk LeeGokul BoyapatiKi Bang SongSang Ki RheeChul Ho Kim

Publisher 

Elsevier

Issue Date 

2000

Citation 

Journal of Bioscience and Bioengineering, vol. 90, no. 6, pp. 684-687

Keywords 

(R)-β-acetylmercaptoisobutyric acidesterase geneG-X-S-X-Gnucleotide sequencepseudomonas aeruginosacarboxylesteraseisobutyric acid derivativeacinetobacter calcoaceticusconsensus sequenceenzyme active site

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.

ISSN 

1389-1723

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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