Identification of the active site serine of hormone‐sensitive lipase by site‐directed mutagenesis
Copyright policy )Identification of the active site serine of hormone‐sensitive lipase by site‐directed mutagenesis
The consensus pentapeptide GXSXG is found in virtually all lipases/esterases and generally contains the active site serine. The primary sequence of hormone‐sensitive lipase contains a single copy of this pentapeptide, surrounding Ser‐423. We have analyzed the catalytic role of Ser‐423 by site‐directed mutagenesis and expression of the mutant hormone‐sensitive lipase in COS cells. Substitution of Ser‐423 by several different amino acids resulted in the complete abolition of both lipase and esterase activity, whereas mutation of other conserved serine residues had no effect on the catalytic activity. These results strongly suggest that Ser‐423 is the active site serine of hormone‐sensitive lipase.
- University of California, Los Angeles United States
- Lund University Sweden
- United States Department of Veterans Affairs United States
- 451 Research (United Kingdom) United Kingdom
Site-directed mutagenesis, Binding Sites, Active site, Blotting, Western, Molecular Sequence Data, Lipase, Sterol Esterase, Transfection, Polymerase Chain Reaction, Peptide Fragments, Cell Line, Rats, Structure-Activity Relationship, Mutagenesis, Site-Directed, Serine, Animals, Amino Acid Sequence
Site-directed mutagenesis, Binding Sites, Active site, Blotting, Western, Molecular Sequence Data, Lipase, Sterol Esterase, Transfection, Polymerase Chain Reaction, Peptide Fragments, Cell Line, Rats, Structure-Activity Relationship, Mutagenesis, Site-Directed, Serine, Animals, Amino Acid Sequence
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