{PDOC00842}
{PS01098; LIPASE_GDSL_SER}
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* Lipolytic enzymes "G-D-S-L" family, serine active site *
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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.

-Consensus pattern: [LIVMFYAG](4)-G-D-S-[LIVM]-x(1,2)-[TAG]-G
                    [S is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: 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.; upton@sol.uvic.ca
           Buckley J.T.; tbuckley@sol.uvic.ca

-Last update: November 1995 / First entry.

[ 1] Upton C., Buckley J.T.
     "A new family of lipolytic enzymes?"
     Trends Biochem. Sci. 20:178-179(1995).
     PubMed=7610479

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