%0 Journal Article
%T Biochemical Characterization of a Novel ¦Á/¦Â-Hydrolase/FSH from the White Shrimp Litopenaeus vannamei
%J Biomolecules | An Open Access Journal from MDPI
%D 2019
%R https://doi.org/10.3390/biom9110674
%X (1) Background: Lipases and esterases are important enzymes that share the ¦Á/¦Â hydrolase fold. The activity and cellular localization are important characteristics to understand the role of such enzymes in an organism. (2) Methods: Bioinformatic and biochemical tools were used to describe a new ¦Á/¦Â hydrolase from a Litopenaeus vannamei transcriptome (LvFHS for Family Serine Hydrolase). (3) Results: The enzyme was obtained by heterologous overexpression in Escherichia coli and showed hydrolytic activity towards short-chain lipid substrates and high affinity to long-chain lipid substrates. Anti-LvFHS antibodies were produced in rabbit that immunodetected the LvFSH enzyme in several shrimp tissues. (4) Conclusions: The protein obtained and analyzed was an ¦Á/¦Â hydrolase with esterase and lipase-type activity towards long-chain substrates up to 12 carbons; its immunodetection in shrimp tissues suggests that it has an intracellular localization, and predicted roles in energy mobilization and signal transduction. View Full-Tex
%U https://www.mdpi.com/2218-273X/9/11/674