Biochemical Characterization of a Novel α/β-Hydrolase/FSH from the White Shrimp Litopenaeus vannamei

(1) Background: Lipases and esterases are important enzymes that share the α/β 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 α/β...

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Published in:Biomolecules (Basel, Switzerland) Vol. 9; no. 11; p. 674
Main Authors: Garcia-Orozco, Karina D, Cinco-Moroyoqui, Francisco, Angulo-Sanchez, Lucía T, Marquez-Rios, Enrique, Burgos-Hernandez, Armando, Cardenas-Lopez, Jose L, Gomez-Aguilar, Carolina, Corona-Martinez, David O, Saab-Rincon, Gloria, Sotelo-Mundo, Rogerio R
Format: Journal Article
Language:English
Published: Switzerland MDPI 31-10-2019
MDPI AG
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Summary:(1) Background: Lipases and esterases are important enzymes that share the α/β 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 α/β hydrolase from a transcriptome (LvFHS for Family Serine Hydrolase). (3) Results: The enzyme was obtained by heterologous overexpression in 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 α/β 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.
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ISSN:2218-273X
2218-273X
DOI:10.3390/biom9110674