Any feedback?
Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Burkholderia cepacia and UniProt Accession P22088
for references in articles please use BRENDA:EC3.1.1.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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: Burkholderia cepacia
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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
activity required deprotonation of the catalytic His residue
triacylglycerol + H2O = diacylglycerol + a carboxylate
the catalytic center is formed by Ser87, Asp264 and His285
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
(R,S)-[4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one + isopropenyl acetate
(R)-(+)-[4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one + (S)-(-)-[4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-acetyloxy-2H-pyran-2-one + prop-1-en-2-ol
-
-
-
-
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
-
-
-
-
?
cis-3-(acetyloxy)-4-phenyl-2-azetidinone + H2O
(3R,4S)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone + (3S,4R)-cis-3-hydroxy-4-phenyl-2-azetidinone + acetate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
in n-heptane
-
?
additional information
?
-
substrate specificity for saturated fatty acids from C6 to C12 and unsaturated long-chain fatty acids. Monoglycerides are hydrolyzed very slowly
-
-
?
additional information
?
-
-
substrate specificity for saturated fatty acids from C6 to C12 and unsaturated long-chain fatty acids. Monoglycerides are hydrolyzed very slowly
-
-
?
additional information
?
-
-
substrate specificity of the extracellular enzyme
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
paraoxon
inhibition of the lipase activities toward emulsified triolein and dissolved p-nitrophenyl acetate by a 1000fold molar excess of paraoxon, 1 h, 99% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methoxypolyethylene glycol
-
enhancement of catalytic activity (up to 3.7fold in neat organic solvent) in the presence of MePEG
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10.5
pH profile, the enzyme is active under acidic conditions and shows 25.3% of maximal activity at pH 4.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in conditions from which the open, active conformation of the enzyme is expected. Its three-dimensional structure is determined independently in three different laboratories and is compared with the closed conformations of the closely related lipases from Pseudomonas glumae and Chromobacterium viscosum
to establish the best crystallization conditions, the hanging-drop method was used (room temperature). Crystals suitable for X-ray diffraction grow in sitting drops. The lipase crystallizes with different salts and ethylene glycol polymers in the presence of n-octyl-beta-D-glucopyranoside and one alkyloligooxyethylene compound in the range from C5E2 to C8E4. The crystals diffract to a resolution of about 0.25 nm. They belong to space group C2 with lattice constants of a = 9.27 nm, b = 4.74 nm, c = 8.65 nm, and beta = 122.3°, indicating a cell content of one molecule per asymmetric unit of the crystal
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10
stable up to 12 h at pH 9 and 10, loses up to 50% activity after 12 h at pH 8
691405
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
30 - 70
purified recombinant enzyme, stable within this range, 96.2% and 86.1% remaining activity after incubated at 70 °C for 2 h and 10 h, respectively
30 - 70
purified recombinant enzyme, stable within this range, 96.2% and 86.1% remaining activity after incubated at 70°C for 2 h and 10 h, respectively
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
22°C, crude enzyme is significantly more resistant to higher concentrations of ethanol (above 40%) than to lower concentrations (20%), whereas purified lipase is inactivated by concentrations of above 40%
amyl alcohol
48 h, 92.5% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
Ethanol
48 h, stable, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
Glycerol
48 h, stable, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
isopropanol
48 h, 91.7% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
Methanol
48 h, 98.34% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
n-heptane
-
enzyme performs the hydrolysis of 4-nitrophenyl palmitate in n-heptane
n-propanol
48 h, 93.5% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
Triton X-100
stable in the presence of the detergent Triton X-100
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromatography on Q-Sepharose in the presence of n-octyl-beta-D-glucopyranoside, Ca2+ precipitation of fatty acids, and octyl-Sepharose chromatography
ammonium sulfate precipitation and Macro-Prep methyl column chromatography
chitin column chromatography and chitosan affinity precipitation (0.3 (w/v) chitosan is required for obtaining maximum active enzyme)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain ER2566 as recombinant enzyme with intein tag
-
gene lipA, DNA and amino acid sequence determination and anaylsis, co-expression of lipA and lipB in Burkholderia cepacia strain G63
gene lipB, DNA and amino acid sequence determination and anaylsis, co-expression of lipA and lipB in Burkholderia cepacia strain G63
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the intein tag is cleaved with dithiothreitol and the refolded lipase is obtained in active form (activity recovery of 80%)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
production of (3R,4S)-cis-azetidinone acetate, which is an intermediate for the synthesis of paclitaxel
synthesis
-
production of [4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one acetate, which is a hydroxymethyl glutaryl coenzyme A (HMG-CoA) reductase inhibitor and a potential anticholesterol drug candidate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, K.K.; Song, H.K.; Shin, D.H.; Hwang, K.Y.; Suh, S.W.
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor
Structure
5
173-185
1997
Burkholderia cepacia
Jger, K.E.; Steinbuechel, A.; Jendrossek, D.
Substrate specificities of bacterial polyhydroxyalkanoate depolymerases and lipases: bacterial lipases hydolyze poly(omega-hydroxyalkanoates)
Appl. Environ. Microbiol.
61
3113-3118
1995
Bacillus subtilis, Burkholderia cepacia, Pseudomonas aeruginosa, Pseudomonas alcaligenes, Pseudomonas fluorescens
Sharma, R.; Chisti, Y.; Banerjee, U.C.
Production, purification, characterization, and applications of lipases
Biotechnol. Adv.
19
627-662
2001
Acinetobacter calcoaceticus, Aspergillus niger, Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus sp. (in: Bacteria), Burkholderia cepacia, Burkholderia sp., Moesziomyces antarcticus, Diutina rugosa, Rhizomucor miehei, Penicillium roqueforti, Hyphopichia burtonii, Proteus vulgaris, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas alcaligenes, Pseudomonas oleovorans, Rhizopus arrhizus, Rhodotorula glutinis, Staphylococcus epidermidis, Penicillium wortmanii, Penicillium roqueforti IAM7268, Bacillus sp. (in: Bacteria) J33, Acinetobacter calcoaceticus BD 413, Geobacillus stearothermophilus L1, Pseudomonas sp. KM1-56
Patel, R.N.
Stereoselective biotransformations in synthesis of some pharmaceutical intermediates
Adv. Appl. Microbiol.
43
91-140
1997
Burkholderia cepacia
Patel, R.N.; Banerjee, A.; Ko, R.Y.; Howell, J.M.; Li, W.S.; Comezoglu, F.T.
Enzymic preparation of (3R-cis)-3-acetyloxy-4-phenyl-2-azetidinone: a taxol side-chain synthon
Biotechnol. Appl. Biochem.
20
23-33
1994
Burkholderia cepacia
-
Poulsen, K.R.; Snabe, T.; Petersen, E.I.; Fojan, P.; Neves-Petersen, M.T.; Wimmer, R.; Petersen, S.B.
Quantization of pH: evidence for acidic activity of triglyceride lipases
Biochemistry
44
11574-11580
2005
Fusarium solani, Rhizomucor miehei, Thermomyces lanuginosus (O59952), Thermomyces lanuginosus, Burkholderia cepacia (P22088), Burkholderia cepacia
Yang, J.; Guo, D.; Yan, Y.
Cloning, expression and characterization of a novel thermal stable and short-chain alcohol tolerant lipase from Burkholderia cepacia strain G63
J. Mol. Catal. B
45
91-96
2007
Burkholderia cepacia (A0EJ12), Burkholderia cepacia (Q4JL88)
-
Singh, P.K.; Gupta, M.N.
Simultaneous refolding and purification of a recombinant lipase with an intein tag by affinity precipitation with chitosan
Biochim. Biophys. Acta
1784
1825-1829
2008
Burkholderia cepacia
Dalal, S.; Singh, P.K.; Raghava, S.; Rawat, S.; Gupta, M.N.
Purification and properties of the alkaline lipase from Burkholderia cepacia A.T.C.C. 25609
Biotechnol. Appl. Biochem.
51
23-31
2008
Burkholderia cepacia (A9QXC9), Burkholderia cepacia
Secundo, F.; Barletta, G.; Mazzola, G.
Role of methoxypolyethylene glycol on the hydration, activity, conformation and dynamic properties of a lipase in a dry film
Biotechnol. Bioeng.
101
255-262
2008
Burkholderia cepacia
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
Kordel, M.; Hofmann, B.; Schomburg, D.; Schmid, R.D.
Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X-ray diffraction data
J. Bacteriol.
173
4836-4841
1991
Burkholderia cepacia (P22088), Burkholderia cepacia, Burkholderia cepacia ATCC 21808 (P22088)
Schrag, J.D.; Li, Y.; Cygler, M.; Lang, D.; Burgdorf, T.; Hecht, H.J.; Schmid, R.; Schomburg, D.; Rydel, T.J.; Oliver, J.D.; Strickland, L.C.; Dunaway, C.M.; Larson, S.B.; Day, J.; McPherson, A.
The open conformation of a Pseudomonas lipase
Structure
15
187-202
1997
Burkholderia cepacia (P22088), Burkholderia cepacia, Burkholderia cepacia ATCC 21808 (P22088)
EXTERNAL LINKS (specific for EC-Number 3.1.1.3)
Transporter Classification Database (TCDB): 8.A.178.1.1, 1.A.115.1.1
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
