The following lipolytic enzymes are evolutionary related:

• 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.

These enzymes contain a Ser-centred consensus sequence and a conserved His-Gly dipeptide found in most lipase N-terminal domains. These sequences are involved in the lipase active site conformation since substitution of the conserved Ser or His residues by Ala and Gln, respectively, results in theloss of both lipase and esterase activities [1].

This entry represents a conserved region containing the putative His active site.

1. Nucleotide sequence of the lipase gene lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues. DNA Cell Biol. 10, 381-8

The following lipolytic enzymes are evolutionary related:

• Mammalian hormone sensitive
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