Cloning and characterization of the lipase and lipase activator protein from Vibrio vulnificus CKM-1

Jer Horng Su; Ming Chung Chang; Yeong Sheng Lee; I Cheng Tseng; Yin Ching Chuang

doi:10.1016/j.bbaexp.2004.01.003

Cloning and characterization of the lipase and lipase activator protein from Vibrio vulnificus CKM-1

Biochim Biophys Acta. 2004 Apr 16;1678(1):7-13. doi: 10.1016/j.bbaexp.2004.01.003.

Authors

Jer Horng Su¹, Ming Chung Chang, Yeong Sheng Lee, I Cheng Tseng, Yin Ching Chuang

Affiliation

¹ Department of Biochemistry, Medical College, National Cheng Kung University, Tainan, Taiwan.

PMID: 15093133
DOI: 10.1016/j.bbaexp.2004.01.003

Abstract

The gene (lipA) encoding the extracellular lipase and its downstream gene (lipB) from Vibrio vulnificus CKM-1 were cloned and sequenced. Nucleotide sequence analysis and alignments of amino acid sequences suggest that Lip Ais a member of bacterial lipase family I.1 and that LipB is a lipase activator of LipA. The active LipA was produced in recombinant Escherichia coli cells only in the presence of the lipB. In the hydrolysis of p-nitrophenyl esters and triacylglycerols, using the reactivated LipA, the optimum chain lengths for the acyl moiety on the substrate were C14 for ester hydrolysis and C10 to C12 for triacylglycerol hydrolysis.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Bacterial Proteins / genetics*
Base Sequence
Cloning, Molecular
Escherichia coli / genetics
Genes, Bacterial
Lipase / genetics*
Molecular Sequence Data
Sequence Alignment
Substrate Specificity
Vibrio vulnificus / genetics*

Substances

Bacterial Proteins
lipase activator protein, Bacteria
Lipase

Associated data

GENBANK/AF436892