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.
PROSITE methods (with tools and information) covered by this documentation:
References
1
Authors
Bairoch A.
Source
Unpublished observations (1995).
2
Authors
Feller G. Thiry M. Gerday C.
Title
Nucleotide sequence of the lipase gene lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues.
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