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Hydrolases & Lipases C

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

Overview

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Listed in this section are hydrolases not accumulated in other parts of the Concise Guide, such as monoacylglycerol lipase and acetylcholinesterase. Pancreatic lipase is the predominant mechanism of fat digestion in the alimentary system; its inhibition is associated with decreased fat absorption. CES1 is present at lower levels in the gut than CES2 (P23141), but predominates in the liver, where it is responsible for the hydrolysis of many aliphatic, aromatic and steroid esters. Hormone-sensitive lipase is also a relatively non-selective esterase associated with steroid ester hydrolysis and triglyceride metabolism, particularly in adipose tissue. Endothelial lipase is secreted from endothelial cells and regulates circulating cholesterol in high density lipoproteins.

Enzymes

3253
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AChE (acetylcholinesterase (Yt blood group)) C Show summary » More detailed page go icon to follow link

BChE (butyrylcholinesterase) C Show summary » More detailed page go icon to follow link

DAGLα (diacylglycerol lipase α) C Show summary » More detailed page go icon to follow link

DAGLβ (diacylglycerol lipase β) C Show summary » More detailed page go icon to follow link

CES1 (carboxylesterase 1) C Show summary » More detailed page go icon to follow link

NTPDase-1 (ectonucleoside triphosphate diphosphohydrolase 1 / CD39) C Show summary » More detailed page go icon to follow link

NTPDase-2 (ectonucleoside triphosphate diphosphohydrolase 2 / CD39L1) C Show summary » More detailed page go icon to follow link

epoxide hydrolase 2 Show summary » More detailed page go icon to follow link

FAAH (Fatty acid amide hydrolase) C Show summary » More detailed page go icon to follow link

Leukotriene A4 hydrolase C Show summary » More detailed page go icon to follow link

LIPE (lipase E, hormone sensitive type) C Show summary » More detailed page go icon to follow link

LIPG (lipase G, endothelial type) C Show summary » More detailed page go icon to follow link

MAGL (monoacylglycerol lipase) C Show summary » More detailed page go icon to follow link

nudix hydrolase 7 Show summary » More detailed page go icon to follow link

neuraminidase 1 Show summary »

neuraminidase 2 Show summary »

O-GlcNAcase Show summary » More detailed page go icon to follow link

PNLIP (pancreatic lipase) C Show summary » More detailed page go icon to follow link

patatin like phospholipase domain containing 2 Show summary »


Target Id 3253
Nomenclature patatin like phospholipase domain containing 2
Previous and unofficial names adipose triglyceride lipase | ATGL | desnutrin
Genes PNPLA2 (Hs), Pnpla2 (Mm), Pnpla2 (Rn)
Ensembl ID ENSG00000177666 (Hs), ENSMUSG00000025509 (Mm), ENSRNOG00000018736 (Rn)
UniProtKB AC Q96AD5 (Hs), O89080 (Mm), P0C548 (Rn)
EC number
3.1.1.3
Inhibitors
atglistatin pIC50 6.2 [31]
Comment This lipase is commonly called ATGL (adipose triglyceride lipase). It generates diacylglycerol from triacylglycerols, which is subsequently degraded to glycerol and fatty acids by hormone-sensitive lipase (HSL; LIPE) and monoglyceride lipase (MGL; MGLL). Lipases including PLA2 and lipases associated with intracellualr lipid droplets (e.g. ATGL, MGLL, FAAH), have been identified as potential molecular targets whose inhibition might provide an antiviral action against infections by RNA viruses (such as SARS-CoV-2 and influenza A virus) in humans [4]. Inhibition of lipase activity is hypothesised to reduce the supply of intracellular free fatty acids upon which the viruses rely for replication, in host cells that are driven to use lipolytic catabolism as a source of free fatty acids and energy in response to virus-induced disruption of normal cellular functions [15].

PLA2-G7 Show summary » More detailed page go icon to follow link

sPLA2-2A Show summary » More detailed page go icon to follow link

PLD2 C Show summary » More detailed page go icon to follow link

vanin 1 Show summary » More detailed page go icon to follow link

Further reading

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References

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NC-IUPHAR subcommittee and family contributors

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How to cite this family page

Database page citation (select format):

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Fabbro D, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Enzymes. Br J Pharmacol. 180 Suppl 2:S289-373.