PROSITE documentation PDOC00903
Lipolytic enzymes "G-D-X-G" family, putative active sites signatures


The following lipolytic enzymes are evolutionary related [1]:

  • Mammalian hormone sensitive lipase (HSL). In adipose tissue and heart, HSL primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production.
  • Mammalian arylacetamide deacetylase (DAC).
  • Moraxella strain TA144 lipase 2 (gene lip2), an enzyme active at a low temperature.
  • Acinetobacter calcoaceticus esterase which seems to be active on simple triglycerides such as triacetin.
  • Streptomyces hygroscopicus acetyl-hydrolase (gene bah), which removes the N-acetyl group from the antibiotic bialaphos.
  • Escherichia coli acetyl esterase aes.

In Moraxella lip2, the mutagenesis [2] of either an histidine or a serine results in the loss of the activity of the enzyme. These putative active site residues are each centered in conserved regions that can be used as signature patterns.

Last update:

April 2006 / Patterns revised.


Technical section

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

LIPASE_GDXG_HIS, PS01173; Lipolytic enzymes "G-D-X-G" family, putative histidine active site  (PATTERN)

LIPASE_GDXG_SER, PS01174; Lipolytic enzymes "G-D-X-G" family, putative serine active site  (PATTERN)


1AuthorsBairoch A.
SourceUnpublished observations (1995).

2AuthorsFeller G. Thiry M. Gerday C.
TitleNucleotide sequence of the lipase gene lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues.
SourceDNA Cell Biol. 10:381-388(1991).
PubMed ID1907455

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