Cloning and characterization of the lipase and lipase activator protein from Vibrio vulnificus CKM-1.
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.
Su
Jer Horng
JH
Department of Biochemistry, Medical College, National Cheng Kung University, Tainan, Taiwan.
Chang
Ming Chung
MC
Lee
Yeong Sheng
YS
Tseng
I Cheng
IC
Chuang
Yin Ching
YC
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D008049:Lipase / Q000235:genetics*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013379:Substrate Specificity; D041261:Vibrio vulnificus / Q000235:genetics*
D001426:Bacterial Proteins; C088618:lipase activator protein, Bacteria; D008049:Lipase