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Information on EC 3.1.1.3 - triacylglycerol lipase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.3 triacylglycerol lipase
IUBMB 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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This record set is specific for:
UNIPROT: Q9RBY1
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
lipase, acyltransferase, pancreatic lipase, hepatic lipase, adipose triglyceride lipase, cholesterol esterase, lipase b, triglyceride lipase, tgl, diacylglycerol lipase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
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-
-
-
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
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-
-
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Triacylglycerol lipase
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-
-
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tributyrase
-
-
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tributyrinase
-
-
-
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triglyceridase
-
-
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triglyceride hydrolase
-
-
-
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triglyceride lipase
-
-
-
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triolein hydrolase
-
-
-
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tween hydrolase
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-
-
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tween-hydrolyzing esterase
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-
-
-
Tweenase
-
-
-
-
additional information
enzyme belongs to the lipase family I.3
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
show the reaction diagram
Ser207 is an active site serine
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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 hide
9001-62-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
low activity
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
show the reaction diagram
high activity
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
show the reaction diagram
high activity
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
show the reaction diagram
high activity
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
show the reaction diagram
high activity
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
high activity
-
?
glyceryl triacetate + H2O
glyceryl diacetate + acetic acid
show the reaction diagram
-
-
?
glyceryl tributyrate + H2O
glyceryl dibutyrate + butyric acid
show the reaction diagram
-
-
?
glyceryl tricaproate + H2O
glyceryl dicaproate + caproic acid
show the reaction diagram
-
-
?
glyceryl tricaprylate + H2O
glyceryl dicaprylate + caprylic acid
show the reaction diagram
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
at least 12 Ca2+ are very tightly bound to one molecule of holoenzyme, which cannot be removed by dialysis but by EDTA treatment, absolutely required for activity, cannot be substituted by other divalent metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chymotrypsin
partial proteolytic digestion of the recombinant enzyme
-
EDTA
removal of bound Ca2+ ions inactivates the enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
purified recombinant enzyme, substrate 4-nitrophenyl butyrate
110
purified recombinant enzyme, substrate 4-nitrophenyl caprate
25
purified recombinant enzyme, substrate 4-nitrophenyl myristate
2500
purified recombinant enzyme, substrate tricaprylate
2600
purified recombinant enzyme, substrate tricaproate
2800
purified recombinant enzyme, substrate olive oil
3
purified recombinant enzyme, substrate 4-nitrophenyl palmitate
30
purified recombinant enzyme, substrate 4-nitrophenyl caproate
3600
purified recombinant enzyme, substrate tributyrate
400
purified recombinant enzyme, substrate triacetate
6
purified recombinant enzyme, substrate 4-nitrophenyl acetate
64
purified recombinant enzyme, substrate 4-nitrophenyl caprylate
72
purified recombinant enzyme, substrate 4-nitrophenyl laurate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme PML, contains the GXSXG motif
SwissProt
Manually annotated by BRENDA team
enzyme PML, contains the GXSXG motif
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9RBY1_9PSED
617
0
64513
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
1 * 66000, SDS-PAGE
68000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 66000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S207A
site-directed mutagenesis, mutation of Ser207, located within the GXSXG motif of serine esterases, leads to inactivation of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from overexpressing Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, overexpression in Escherichia coli, enzyme forms inclusion bodies
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme in inclusion bodies is solubilized by 8 M urea and refolded by removing urea in presence of Ca2+
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Amada, K.; Haruki, M.; Imanaka, T.; Morikawa, M.; Kanaya, S.
Overproduction in Escherichia coli, purification and characterization of a family I.3 lipase from Pseudomonas sp. MIS38
Biochim. Biophys. Acta
1478
201-210
2000
Pseudomonas sp. (Q9RBY1), Pseudomonas sp., Pseudomonas sp. MIS38 (Q9RBY1)
Manually annotated by BRENDA team