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Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Sus scrofa and UniProt Accession P00591
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3.1.1.3 triacylglycerol lipaseIUBMB Comments
The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
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Word Map
- 3.1.1.3
- amylase
- lipoprotein
- pancreas
- triacylglycerols
-
lipolytic
- phospholipid
- antarctica
- esterification
- obesity
- abdominal
- hdl
-
biocatalyst
-
apolipoproteins
- pain
-
exocrine
- adipocytes
-
oleic
- milk
-
cholesteryl
- droplet
- palmitate
- meal
- phosphatidylcholine
-
high-density
- p-nitrophenyl
-
hormone-sensitive
- olive
-
acinar
- duodenal
-
enantioselectivity
-
obese
- hypertriglyceridemia
-
interfacial
-
phosphatidic
-
esterify
-
micelle
- juice
-
arachidonic
-
emulsify
- oleate
-
postprandial
-
endoscopic
- cholecystokinin
-
reusable
- lecithin
- hexane
-
endocannabinoids
-
hdl-cholesterol
- taurocholate
- trypsinogen
- detergent
- synthesis
- paper production
- nutrition
- food industry
- environmental protection
- biofuel production
- medicine
- biotechnology
The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipase, acyltransferase, pancreatic lipase, hepatic lipase, adipose triglyceride lipase, cholesterol esterase, lipase b, triglyceride lipase, tgl, diacylglycerol lipase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amano AP
-
-
-
-
amano B
-
-
-
-
amano CE
-
-
-
-
amano CES
-
-
-
-
amano P
-
-
-
-
amno N-AP
-
-
-
-
BAL
-
-
-
-
Bile-salt-stimulated lipase
-
-
-
-
BSSL
-
-
-
-
butyrinase
-
-
-
-
cacordase
-
-
-
-
CALB
-
-
-
-
capalase L
-
-
-
-
Carboxyl ester lipase
-
-
-
-
cholesterol esterase
-
-
-
-
Cytotoxic T lymphocyte lipase
-
-
-
-
EDL
-
-
-
-
endothelial cell-derived lipase
-
-
-
-
endothelial-derived lipase
-
-
-
-
GA 56 (enzyme)
-
-
-
-
Gastric lipase
-
-
-
-
GEH
-
-
-
-
glycerol ester hydrolase
-
-
-
-
glycerol-ester hydrolase
-
-
-
-
heparin releasable hepatic lipase
-
-
-
-
hepatic lipase
-
-
-
-
hepatic monoacylglycerol acyltransferase
-
-
-
-
Lingual lipase
-
-
-
-
lipase
lipase, triacylglycerol
-
-
-
-
lipazin
-
-
-
-
liver lipase
-
-
-
-
meito MY 30
-
-
-
-
meito Sangyo OF lipase
-
-
-
-
Pancreatic lipase
Pancreatic lysophospholipase
-
-
-
-
PGE
-
-
-
-
PL-RP2
-
-
-
-
post-heparin plasma protamine-resistant lipase
-
-
-
-
PPL
-
-
-
-
Pregastric esterase
-
-
-
-
Pregastric lipase
-
-
-
-
salt-resistant post-heparin lipase
-
-
-
-
steapsin
-
-
-
-
Sterol esterase
-
-
-
-
takedo 1969-4-9
-
-
-
-
teenesterase
-
-
-
-
tiacetinase
-
-
-
-
tibutyrin esterase
-
-
-
-
triacylglycerol ester hydrolase
-
-
-
-
Triacylglycerol lipase
-
-
-
-
tributyrase
-
-
-
-
tributyrinase
-
-
-
-
triglyceridase
-
-
-
-
triglyceride hydrolase
-
-
-
-
triglyceride lipase
-
-
-
-
triolein hydrolase
-
-
-
-
tween hydrolase
-
-
-
-
tween-hydrolyzing esterase
-
-
-
-
Tweenase
-
-
-
-
lipase
-
-
-
-
Pancreatic lipase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases
-
triacylglycerol + H2O = diacylglycerol + a carboxylate
ping pong bi bi kinetic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
triacylglycerol acylhydrolase
The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
CAS REGISTRY NUMBER
COMMENTARY
9001-62-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2 di-O-lauryl-rac-glycero-3-(glutaric acid 6-methyl) resorufin ester + H2O
?
-
-
-
-
?
triolein + H2O
diolein + oleate
-
substrate is an olive oil/gum arabic emulsion containing radiolabeled triolein in presence of bile acids and lecithin at rate-limiting concentrations, rapid exchange of the enzyme between two different triacylglycerol droplets measured by a non-exchanging enzyme inhibitor in one of the droplets
-
-
?
additional information
?
-
-
methyl esters are cleaved by lipase 5 times faster than ethyl esters. The relative hydrolysis rates are rather low for esters of C3 and C4 alcohols, they increase abruptly for esters of n-hexyl alcohol, which are cleaved faster than methyl esters
-
-
?
additional information
?
-
-
enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide
-
?
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
additional information
?
-
-
pancreatic lipase-catalyzed esterification of n-butanoic acid in solvent-free system and in isooctane carried out with three alcohols: n-pentanol, n-heptanol and geraniol, overview, substrate polarity has an effect on the lipase-catalyzed synthesis of aroma esters in solvent-free systems, solvent-free synthesis enzyme inactivation by acid substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alginate
-
alginate inhibits pancreatic lipase by a maximum of 72.2% with synthetic substrate and 58% with natural substrate. High-guluronic acid alginates from Laminaria hyperborea seaweed inhibit pancreatic lipase to a significantly higher degree than high-mannuronic acid alginates from Lessonia nigrescens
diethyl 4-nitrophenyl phosphate
-
diethyl 4-nitrophenyl phosphate is only ìnhibitory in the presence of deoxycholic acid sodium salt (2 mM)
lysophosphatidylcholine
-
increases Km and reduces Vmax of the enzyme with triaclyglyrol substrates, not with monoacylglycerols, the activity is completely restored by addition of taurodeoxycholine or phospholipid
Pectin
-
pectin freshly isolated from citrus segment membranes is a strong inhibitor of lipase activity, commercial citrus pectin shows a weak inhibitory effect (activity is reduced by 20%)
additional information
-
plant extracts from bearberry (Arctostaphylos uva-ursi), garden pea (Pisum sativum), Norway spruce (Picea abies) and large leaved lime (Tilia platyphyllos) show inhibition of pancreatic lipase (over 40%)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Bile salts
-
around 0.2 mM, enhance lipolysis slightly, activation depends on substrate, it is maximal for trihexanoin hydrolysis, no activation of tripropionin hydrolysis
Phospholipid
-
enhances the hydrophobic character of the lipid binding domain of the enzyme responsible for its penetration into organized lipid structure
Colipase
-
increases the activity on short-chain triglycerides, but only at high temperature when lipase denaturation occurs
-
additional information
-
six disulfide bridges and two free thiols: The disulfide bridges form relatively small loops along the main chain
-
additional information
-
active towards triacylglycerols containing short fatty acids from C2 to C6
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics in presence of lysophosphatidylcholine and of taurodeoxycholine
-
additional information
additional information
-
kinetic constants of ester synthesis catalyzed with porcine pancreatic lipase, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
after 23.33fold purification, with tributyrin as substrate, at pH 8.0 and 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the immobilization procedure broadened the pH working range of the free lipase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
activity range of free lipase and immobilized lipase, over 80% of maximal activity at 35°C-55°C of the immobilized lipase
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ATGL expression increases dramatically in the subcutaneous adipose during adipose development and maturation, as well as during in vitro adipogenesis. Within the white adipose tissue, ATGL is expressed at higher levels in the adipocyte than in the stromal-vascular fraction
additional information
-
-
80811, 80812, 80813, 80814, 80815, 80816, 80817, 80818, 80819, 80820, 80821, 80822, 80823, 80824, 80836, 80852, 80853, 664171, 664172, 693794, 693798, 694611, 729305, 729771, 730743
additional information
-
tissue-specific functions, expression is developmentally regulated, detailed overview
additional information
-
analysis of ATGL gene and protein expression in vitro and in vivo, tissue expression analysis, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
ATGL expression reacts to hormonal stimuli and plays a role in catecholamine-induced lipolysis in porcine adipose tissue
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LIPP_PIG
450
0
50084
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
both isoenzymes are glycoproteins containing 3.8 mol of mannose and 2.9 mol of N-acetylglucosamine per mol of enzyme
side-chain modification
-
contains three glucosamine residues and three mannose residues per subunit
side-chain modification
-
isoenzymes Lc and LA1 contain 0.4 M sialic acid per mol of protein, isoenzyme LA2 contains 0.1 M sialic acid per mol of protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
immobilization of the pancreatic lipase on a polysiloxane-polyvinyl alcohol hybrid matrix with 250 U/g matrix, the immobilized enzyme shows high activity converting triglycerides to fatty acid alkyl esters attaining yields varying from 75% to 95%
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6
-
the enzyme loses 70% of its activity at acid pH, after 5 min of incubation
730743
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
the enzyme is unstable at temperatures over 37°C with less than 40% activity at 40°C, about 25% activity at 45°C, and no activity at 50°C, after 30 min of incubation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
colipase and bile salts stabilize the enzyme against inactivation at its water/substrate interface: colipase and bile salts above their critical micellar concentration offer better protection than either of them alone
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATGL gene, DNA and amino acid sequence determination and analysis, tissue expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ATGL transcript levels are hormone sensitive, and are decreased by insulin and forskolin in primary pig preadipocytes
-
peroxisome proliferator-activated receptor gamma transcript levels increase concomitant with ATGL gene expression, suggesting a possible role in the regulation of ATGL by adipogenic regulators
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
application of the immobilized lipase in non-conventional biocatalysis for the synthesis of surfactants and biodiesel, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
O'Connor, K.C.; Bailey, J.E.
Hydrolysis of emulsified tributyrin by porcine pancreatic lipase
Enzyme Microb. Technol.
10
352-356
1988
Sus scrofa
-
Guibe-Jampel, E.; Rousseau, G.; Salaun, J.
Enantioselective hydrolysis of racemic diesters by porcine pancreatic lipase
J. Chem. Soc. Chem. Commun.
1987
1080-1081
1987
Sus scrofa
-
Benkouka, F.; Guidoni, A.A.; de Caro, J.D.; Bonicel, J.J.; Desnuelle, P.A.; Rovery, M.
Porcine pancreatic lipase. The disulfide bridges and the sulfhydryl groups
Eur. J. Biochem.
128
331-341
1982
Sus scrofa
Borgstrm, B.
The temperature-dependent interfacial inactivation of porcine pancreatic lipase. Effect of colipase and bile salts
Biochim. Biophys. Acta
712
490-497
1982
Sus scrofa
De Caro, J.; Boudouard, M.; Bonicel, J.; Guidoni, A.; Desnuelle, G.P.; Rovery, M.
Porcine pancreatic lipase. Complementation of the primary structure
Biochim. Biophys. Acta
71
129-138
1981
Sus scrofa
-
Brockmann, H.L.
Triglyceride lipase from porcine pancreas
Methods Enzymol.
71
619-627
1981
Sus scrofa
Garner, C.W.
Boronic acid inhibitors of porcine pancreatic lipase
J. Biol. Chem.
255
5064-5068
1980
Sus scrofa
Rovery, M.; Boudouard, M.; Bianchetta, J.
An improved large scale procedure for the purification of porcine pancreatic lipase
Biochim. Biophys. Acta
525
373-379
1978
Sus scrofa
Savary, P.
Action of rat pancreatic juice and of purified pig pancreatic lipase upon the esters of short-chain aliphatic monoacids and long-chain primary monoalcohols
Biochim. Biophys. Acta
270
463-471
1972
Rattus norvegicus, Sus scrofa
Maylie, M.F.; Charles, M.; Desnuelle, P.
Action of organophosphates and sulfonyl halides on porcine pancreatic lipase
Biochim. Biophys. Acta
276
162-175
1972
Sus scrofa
Erlanson, C.; Borgstrm, B.
Purification and further characterization of co-lipase from porcine pancreas
Biochim. Biophys. Acta
271
400-412
1972
Sus scrofa
Garner, C.W.; Smith, L.C.
Porcine pancreatic lipase. A glycoprotein
J. Biol. Chem.
247
561-565
1972
Sus scrofa
Malie, M.F.; Charles, M.; Astier, M.; Desnuelle, P.
On porcine pancreatic colipase: large scale purification and some properties
Biochem. Biophys. Res. Commun.
52
291-297
1973
Sus scrofa
Savary, P.
The action of pure pig pancreatic lipase upon esters of long-chain fatty acids and short-chain primary alcohols
Biochim. Biophys. Acta
248
149-155
1971
Sus scrofa
Sikk, P.; Osa, A.; Aaviksaar, A.
Irreversible inhibition of pancreatic lipase by bis-p-nitrophenyl methylphosphonate
FEBS Lett.
184
193-196
1985
Sus scrofa
Granon, S.; Semeriva, M.
Effect of taurodeoxycholate, colipase and temperature on the interfacial inactivation of porcine pancreatic lipase
Eur. J. Biochem.
111
117-124
1980
Sus scrofa
Sugihara, A.; Gargouri, Y.; Pieroni, G.; Riviere, C.; Saeda, L.; Verger, R.
Activities and interfacial properties of Rhizopus delemar and porcine pancreatic lipases after treatment with phospholipids
Biochemistry
25
3430-3434
1986
Rhizopus arrhizus, Sus scrofa
-
David, L.; Guo, X.J.; Villard, C.; Moulin, A.; Puigserver, A.
Purification and molecular cloning of porcine intestinal glycerol-ester hydrolase--evidence for its identity with carboxylesterase
Eur. J. Biochem.
257
142-148
1998
Sus scrofa
Maruyama, T.; Nakajima, M.; Kondo, H.; Kawasaki, K.; Seki, M.; Goto, M.
Can lipases hydrolyze a peptide bond?
Enzyme Microb. Technol.
32
655-657
2003
Bacillus subtilis, Diutina rugosa, Fusarium solani, Homo sapiens, Thermomyces lanuginosus, Rhizomucor miehei, Rhizopus arrhizus, Rhizopus japonicus, Sus scrofa, Chromobacterium viscosum, Alcaligenes ssp., Bacillus subtilis 168 BsL
-
Haiker, H.; Lengsfeld, H.; Hadvary, P.; Carriere, F.
Rapid exchange of pancreatic lipase between triacylglycerol droplets
Biochim. Biophys. Acta
1682
72-79
2004
Homo sapiens, Sus scrofa
Tsuzuki, W.; Ue, A.; Nagao, A.; Endo, M.; Abe, M.
Inhibitory effect of lysophosphatidylcholine on pancreatic lipase-mediated hydrolysis in lipid emulsion
Biochim. Biophys. Acta
1684
1-7
2004
Sus scrofa
Dolinsky, V.W.; Gilham, D.; Alam, M.; Vance, D.E.; Lehner, R.
Triacylglycerol hydrolase: role in intracellular lipid metabolism
Cell. Mol. Life Sci.
61
1633-1651
2004
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Paula, A.V.; Urioste, D.; Santos, J.C.; de Castro, H.F.
Porcine pancreatic lipase immobilized on polysiloxane-polyvinyl alcohol hybrid matrix: catalytic properties and feasibility to mediate synthesis of surfactants and biodiesel
J. Chem. Technol. Biotechnol.
82
281-288
2007
Sus scrofa (P00591)
-
Bezbradica, D.; Mijin, D.; Siler-Marinkovic, S.; Knezevic, Z.
The effect of substrate polarity on the lipase-catalyzed synthesis of aroma esters in solvent-free systems
J. Mol. Catal. B
45
97-101
2007
Rhizomucor miehei, Sus scrofa
-
Edashige, Y.; Murakami, N.; Tsujita, T.
Inhibitory effect of pectin from the segment membrane of citrus fruits on lipase activity
J. Nutr. Sci. Vitaminol.
54
409-415
2008
Sus scrofa
Utsugi, A.; Kanda, A.; Hara, S.
Lipase specificity in the transacylation of triacylglycerin
J. Oleo Sci.
58
123-132
2009
Aspergillus niger, Burkholderia cepacia, Diutina rugosa, Mucor javanicus, Rhizomucor miehei, Penicillium camemberti, Penicillium roqueforti, Pseudomonas fluorescens, Rhizopus arrhizus, Rhizopus niveus, Sus scrofa
Slanc, P.; Doljak, B.; Kreft, S.; Lunder, M.; Janes, D.; Strukelj, B.
Screening of selected food and medicinal plant extracts for pancreatic lipase inhibition
Phytother. Res.
23
874-877
2009
Sus scrofa
Deiuliis, J.A.; Shin, J.; Bae, D.; Azain, M.J.; Barb, R.; Lee, K.
Developmental, hormonal, and nutritional regulation of porcine adipose triglyceride lipase (ATGL)
Lipids
43
215-225
2008
Sus scrofa
Aloulou, A.; Frikha, F.; Noiriel, A.; Bou Ali, M.; Abousalham, A.
Kinetic and structural characterization of triacylglycerol lipases possessing phospholipase A1 activity
Biochim. Biophys. Acta
1841
581-587
2014
Equus caballus, Homo sapiens, Sus scrofa
Wilcox, M.D.; Brownlee, I.A.; Richardson, J.C.; Dettmar, P.W.; Pearson, J.P.
The modulation of pancreatic lipase activity by alginates
Food Chem.
146
479-484
2014
Sus scrofa
EXTERNAL LINKS (specific for EC-Number 3.1.1.3)
Transporter Classification Database (TCDB): 8.A.178.1.1, 1.A.115.1.1
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