PROSITE documentation PDOC00842
Lipolytic enzymes "G-D-S-L" family, serine active site


Recently [1], a family of lipolytic enzymes has been characterized. This family currently consist of the following proteins:

  • Aeromonas hydrophila lipase/phosphatidylcholine-sterol acyltransferase.
  • Xenorhabdus luminescens lipase 1.
  • Vibrio mimicus arylesterase.
  • Escherichia coli acyl-coA thioesterase I (gene tesA).
  • Vibrio parahaemolyticus thermolabile hemolysin/atypical phospholipase.
  • Rabbit phospholipase AdRab-B, an intestinal brush border protein with esterase and phospholipase A/lysophospholipase activity that could be involved in the uptake of dietary lipids. AdRab-B contains four repeats of about 320 amino acids.
  • Arabidopsis thaliana and Brassic napus anther-specific proline-rich protein APG.
  • A Pseudomonas putida hypothetical protein in trpE-trpG intergenic region.

A serine has been identified a part of the active site in the Aeromonas, Vibrio mimicus and Escherichia coli enzymes. It is located in a conserved sequence motif that can be used as a signature pattern for these proteins.


This pattern will pick up two of the four repeats in AdRab-B, the first one is not detected as its sequence has diverged in the region of the putative active site residue. The last one is also not detected because it is slightly divergent at the end of the pattern.

Expert(s) to contact by email:

Upton C.
Buckley J.T.

Last update:

November 1995 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LIPASE_GDSL_SER, PS01098; Lipolytic enzymes "G-D-S-L" family, serine active site  (PATTERN)


1AuthorsUpton C. Buckley J.T.
TitleA new family of lipolytic enzymes?
SourceTrends Biochem. Sci. 20:178-179(1995).
PubMed ID7610479

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