원문정보
초록
영어
The GDSL enzymes are composed of various structural α/β hydrolases fold and they have an activity in lipases, esterases, tioesterases, arylesterases, proteases and lysophospholiases. This family has conserved amino acid sequences which is composed of glycine (G), aspartate (D), serine (S), and leucine (L) in N-terminal region in blocks I, II, III, and V in five sequence. Most especially, the nucleophilic serine is located in active site nearby N-terminal region. This serine is found in the sequence G-X-S-X-G, which accounts for the turn and is considered to be as one of the identifying features of these enzymes. Here, we investigated the structural and functional properties of GDSL enzymes with specific emphasis on the recently-known Sm23. Structural and functional comparisons with other GDSL enzymes and alpha/beta hydrolase were done for its engineering applications.