{PDOC00903} {PS01173; LIPASE_GDXG_HIS} {PS01174; LIPASE_GDXG_SER} {BEGIN} ************************************************************************ * 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. -Consensus pattern: [LIVMF](2)-x-[LIVMF]-H-G(2)-[SAG]-[FYW]-x(3)-[STDN]- x(1,2)-[STYA]-[HAGFT] [The first H may be an active site residue] -Sequences known to belong to this class detected by the pattern: ALL, except for DAC. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [LIVM]-x-[LIVMF]-[SA]-G-D-S-[CAS]-G-[GA]-x-[LI]-[CAVT] [S may be an active site residue] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2006 / Patterns revised. [ 1] Bairoch A. Unpublished observations (1995). [ 2] Feller G., Thiry M., Gerday C. "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. 10:381-388(1991). PubMed=1907455; -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}