LYPLAL1 Human

The LYPLAL1 gene is located on chromosome 1q41 . The protein shares structural similarities with acyl protein thioesterases (APTs), featuring a typical alpha/beta hydrolase fold and a classical catalytic triad of serine, aspartate, and histidine . However, unlike other APT family members, LYPLAL1’s hydrophobic tunnel is closed, and it functions as a monomer rather than a dimer .

Using an in vitro assay of recombinant human LYPLAL1 expressed in Escherichia coli, researchers found that LYPLAL1 showed no phospholipase activity. Instead, it hydrolyzed short-chain substrates such as 4-nitrophenyl acetate . The crystal structure of human LYPLAL1 at 1.72-angstrom resolution revealed its functional plasticity despite its close relationship to acyl protein thioesterases .

LYPLAL1’s primary function is to hydrolyze short-chain substrates, which distinguishes it from other members of the AB hydrolase 2 family . This unique functionality is attributed to its shallow active site, which limits its activity to short-chain substrates .

The study of LYPLAL1 has provided valuable insights into the functional diversity of the AB hydrolase 2 family. Understanding its structure and function can aid in the development of targeted therapies and biotechnological applications. For instance, the recombinant expression of LYPLAL1 in E. coli has facilitated detailed biochemical studies and potential industrial applications .