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Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Bos taurus and UniProt Accession Q2KI18
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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: Bos taurus
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
-
-
-
-
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
additional information
?
-
diacylglycerol lipase may regulate protein kinase C activity and 2-arachidonoyl-sn-glycerol levels by rapidly altering the intracellular concentration of diacylglycerols
-
-
?
additional information
?
-
1,2-diacyl-sn-glycerols are the preferred substrates over 1,3-diacyl-sn-glycerols. The enzyme hydrolyzes stearate in preference to palmitate from the sn-1-position of 1,2-diacyl-sn-glycerols. 1-O-alkyl-2-acyl-sn-glycerols are not a substrate for the enzyme
-
-
?
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
-
-
?
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
?
-
diacylglycerol lipase may regulate protein kinase C activity and 2-arachidonoyl-sn-glycerol levels by rapidly altering the intracellular concentration of diacylglycerols
-
-
?
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
tissue-specific functions, expression is developmentally regulated, detailed overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). PLPL2_BOVIN
486
1
53417
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphorylation by cAMP-dependent protein kinase results in a three-fold increase in catalytic thrpoughput
side-chain modification
-
10% carbohydrate, hexosamine is predominantly N-acetylglucosamine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bernbck, S.; Hernell, O.; Blckberg, L.
Purification and molecular characterization of bovine pregastric lipase
Eur. J. Biochem.
148
233-238
1985
Bos taurus
Galatioto, L.E.; Zahler, P.
Characterization of a triacylglycerol lipase that liberates arachidonic acid from bovine chromaffin cells during secretion
J. Neurochem.
60
32-39
1993
Bos taurus
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
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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