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	PROSITE documentation PDOC00110 [for PROSITE entry PS00120]

Lipases, serine active site

Triglyceride lipases (EC 3.1.1.3) [1] are lipolytic enzymes that hydrolyzes the ester bond of triglycerides. Lipases are widely distributed in animals, plants and prokaryotes. In higher vertebrates there are at least three tissue-specific isozymes: pancreatic, hepatic, and gastric/lingual. These three types of lipases are closely related to each other as well as to lipoprotein lipase (EC 3.1.1.34) [2], which hydrolyzes triglycerides of chylomicrons and very low density lipoproteins (VLDL).

The most conserved region in all these proteins is centered around a serine residue which has been shown [3] to participate, with an histidine and an aspartic acid residue, to a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase (EC 2.3.1.43) (LCAT) [4], which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol. We have built a pattern from that region.

Note:

Drosophila vitellogenins are also related to lipases [5], but they have lost their active site serine.

Last update:

December 2004 / Pattern and text revised.

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

LIPASE_SER, PS00120; Lipases, serine active site  (PATTERN)

• Consensus pattern:
  [LIV]-{KG}-[LIVFY]-[LIVMST]-G-[HYWV]-S-{YAG}-G-[GSTAC]
  S is the active site residue
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 289
  • detected by PS00120: 229 (true positives)
  • undetected by PS00120: 60 (53 false negatives and 7 'partials')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00120:
  78 false positives and 27 unknowns.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00120
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00120
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00120
• View ligand binding statistics of PS00120
• Matching PDB structures: 1BU8 1CVL 1DT3 1DT5 ... [ALL]

1	Authors	Chapus C., Rovery M., Sarda L., Verger R.
	Title	Minireview on pancreatic lipase and colipase.
	Source	Biochimie 70:1223-1234(1988).
	PubMed ID	3147715

2	Authors	Persson B., Bengtsson-Olivecrona G., Enerback S., Olivecrona T., Jornvall H.
	Title	Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase.
	Source	Eur. J. Biochem. 179:39-45(1989).
	PubMed ID	2917565

3	Authors	Blow D.
	Title	Enzymology. More of the catalytic triad.
	Source	Nature 343:694-695(1990).
	PubMed ID	2304545
	DOI	10.1038/343694a0

4	Authors	McLean J., Fielding C., Drayna D., Dieplinger H., Baer B., Kohr W., Henzel W., Lawn R.
	Title	Cloning and expression of human lecithin-cholesterol acyltransferase cDNA.
	Source	Proc. Natl. Acad. Sci. U.S.A. 83:2335-2339(1986).
	PubMed ID	3458198

5	Authors	Baker M.E.
	Title	Is vitellogenin an ancestor of apolipoprotein B-100 of human low-density lipoprotein and human lipoprotein lipase?
	Source	Biochem. J. 255:1057-1060(1988).
	PubMed ID	3145737

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