Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC3.1.1.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adipose TG lipase
-
-
adipose triglyceride lipase
-
-
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
-
-
-
-
desnutrin
-
-
EDL
-
-
-
-
endothelial cell-derived lipase
-
-
-
-
endothelial 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
-
-
-
-
hormone sensitive lipase
-
-
hormone-sensitive lipase
-
-
HPLRP2
-
-
Lingual lipase
-
-
-
-
lipase
lipase, triacylglycerol
-
-
-
-
lipazin
-
-
-
-
lipoprotein lipase
-
hydrolyzes triglycerides in chylomicrons and very low density lipoprotein particles
liver lipase
-
-
-
-
meito MY 30
-
-
-
-
meito Sangyo OF lipase
-
-
-
-
Pancreatic lipase
pancreatic lipase-related protein 2
-
-
Pancreatic lysophospholipase
-
-
-
-
pancreatic triacylglycerol lipase
-
pancreatic triglyceride lipase
-
-
PGE
-
-
-
-
phospholipase A2xi
-
-
PL-RP2
-
-
-
-
post-heparin plasma protamine-resistant lipase
-
-
-
-
PPL
-
-
-
-
Pregastric esterase
-
-
-
-
Pregastric lipase
-
-
-
-
salt-resistant post-heparin lipase
-
-
-
-
steapsin
-
-
-
-
Sterol esterase
-
-
-
-
TAG lipase
-
-
takedo 1969-4-9
-
-
-
-
teenesterase
-
-
-
-
TG hydrolase
-
-
TG lipase
-
-
tiacetinase
-
-
-
-
tibutyrin esterase
-
-
-
-
triacylglycerol acylhydrolase
-
-
triacylglycerol ester hydrolase
-
-
-
-
triacylglycerol hydrolase
-
-
Triacylglycerol lipase
-
-
-
-
tributyrase
-
-
-
-
tributyrinase
-
-
-
-
triglyceridase
-
-
-
-
triglyceride hydrolase
-
-
-
-
triglyceride lipase
triolein hydrolase
-
-
-
-
tween hydrolase
-
-
-
-
tween-hydrolyzing esterase
-
-
-
-
Tweenase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
show the reaction diagram
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
2,3-dibutyrylthio-1-propyl oleate + H2O
2,3-dibutyrylthiopropyl alcohol + oleate
show the reaction diagram
-
chromogenic detection using 5,5'-dithio-bis-(2-nitrobenzoic acid) as chromogen or the 6-methylresorufin ester of 1-O,2-dilauryl-rac-glycero-3-glutaric acid, substrate synthesis, assay development, optimization, and method comparison, overview
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
diolein + H2O
monoolein + oleate
show the reaction diagram
-
-
-
-
?
L-alpha-phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
olive oil + H2O
?
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
butyric acid + ?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
show the reaction diagram
tricaprylin + H2O
dicaprylin + caprylate
show the reaction diagram
-
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
show the reaction diagram
-
-
-
-
?
trioctanoin + H2O
octanoic acid + ?
show the reaction diagram
-
-
-
-
?
triolein + H2O
diolein + oleate
show the reaction diagram
trioleoylglycerol + H2O
oleic acid + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
-
recombinant enzyme in Sf9 cells
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Colipase
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates the phospholipase A1 activity of the enzyme, overview
Mg2+
-
-
NaCl
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hexadecenoic acid
-
aurantiamide
-
Bile salts
-
-
cnidiadin
-
orlistat
sodium taurodeoxycholate
-
-
additional information
-
changes in HDL cholesteryl ester and fatty acid content have no effect on hepatic lipase displacement, increases in HDL phospholipid and TG content significantly inhibit hepatic lipase displacement
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bile salt
-
pancreatic lipase, stimulation
CGI-58
-
Colipase
-
dilinoleoylphosphatidylcholine
-
promotes hepatic lipase liberation from cell surface proteoglycans
HDL
-
HDL is able to displace cell surface-bound hepatic lipase and stimulate vascular triglyceride hydrolysis, much like heparin. HDL fractions from hyperlipidemic patients are unable to displace HL from the cell surface
-
heparin
high-density lipoprotein
-
HDL, acts much like heparin to liberate hepatic lipase from cell surface proteoglycans and stimulate triglyceride clearance
-
perilipin A
-
phosphorylation of perilipin specifically at serine 517 by protein kinase A is essential for ATGL activation, overview
-
sodium taurodeoxycholate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
kinetics of beta5'-loop-mediated interaction of the enzyme with the colipase, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
-
purified recombinant mutant enzyme lacking the cap domain, substrate triolein
0.5
-
purified recombinant mutant enzyme lacking the lid domain, substrate triolein
1300
-
purified gastric lipase, substrate tributyrin
15
-
purified pancreatic lipase, solid meal
30
-
purified recombinant wild-type enzyme, substrate triolein
32
-
purified gastric lipase, liquid test meal
34
-
purified gastric lipase, solid test meal
3900
-
purified recombinant wild-type enzyme
43
-
purified pancreatic lipase, liquid meal
51.1
-
-
550
-
purified recombinant enzyme in presence of colipase at pH 8.8
7895
-
-
8000
-
purified pancreaic lipase, substrate tributyrin
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
gastric lipase HGL, assay at
5
-
assay at
6.5 - 7.5
-
pancreatic lipase HPL
7
-
assay at
8
-
assay at
8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
-
additional information
-
pH profiles of the recombinant enzyme, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
gastric lipase HGL
Manually annotated by BRENDA team
-
i.e. RH-17777 cell, large cell lung carcinoma cell line, low enzyme activity
Manually annotated by BRENDA team
-
HSL
Manually annotated by BRENDA team
-
ATGL is highly expressed in the pigment epithelium and can be found on the plasma membrane
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
mainly
Manually annotated by BRENDA team
-
secretion in the stomach
-
Manually annotated by BRENDA team
-
ATGL in the pigment epithelium
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
in ATGL or CGI-58 cause neutral lipid storage disease with myopathy and ichthyosis, respectively, in humans
metabolism
physiological function
additional information
-
HDL particles in plasma are central to regulation of hepatic lipase displacement and the hydrolytic activity of hepatic lipase, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIPG_HUMAN
398
0
45238
Swiss-Prot
Secretory Pathway (Reliability: 2)
CEL_HUMAN
753
0
79322
Swiss-Prot
Secretory Pathway (Reliability: 1)
PLB1_HUMAN
1458
1
163081
Swiss-Prot
Secretory Pathway (Reliability: 1)
PLPL2_HUMAN
504
1
55316
Swiss-Prot
Secretory Pathway (Reliability: 4)
PLPL3_HUMAN
481
0
52865
Swiss-Prot
other Location (Reliability: 4)
PLPL4_HUMAN
253
0
27980
Swiss-Prot
Secretory Pathway (Reliability: 5)
PLPL5_HUMAN
429
0
47912
Swiss-Prot
other Location (Reliability: 1)
DGLB_HUMAN
672
4
73732
Swiss-Prot
Secretory Pathway (Reliability: 2)
LIPP_HUMAN
465
0
51157
Swiss-Prot
Secretory Pathway (Reliability: 2)
LIPR2_HUMAN
469
0
51961
Swiss-Prot
Secretory Pathway (Reliability: 2)
LIPC_HUMAN
499
0
55914
Swiss-Prot
Secretory Pathway (Reliability: 1)
LIPE_HUMAN
500
0
56795
Swiss-Prot
Secretory Pathway (Reliability: 1)
AAAD_HUMAN
399
1
45734
Swiss-Prot
Secretory Pathway (Reliability: 1)
LIPR3_HUMAN
467
0
52254
Swiss-Prot
Secretory Pathway (Reliability: 2)
E9PRT6_HUMAN
467
0
51845
TrEMBL
Secretory Pathway (Reliability: 2)
H7BYX7_HUMAN
1446
1
161636
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1W6R6W1_HUMAN
434
1
47437
TrEMBL
Secretory Pathway (Reliability: 4)
B2RWP8_HUMAN
1458
1
162978
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0K0L4Y0_HUMAN
504
1
55359
TrEMBL
Secretory Pathway (Reliability: 5)
B4DDT1_HUMAN
438
0
48965
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0U1WL47_HUMAN
504
1
55385
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0K0L4Y8_HUMAN
504
1
55350
TrEMBL
Secretory Pathway (Reliability: 4)
Q68D36_HUMAN
118
0
13315
TrEMBL
Secretory Pathway (Reliability: 2)
A0A142EFS1_HUMAN
88
0
9783
TrEMBL
Mitochondrion (Reliability: 5)
Q53F21_HUMAN
398
0
45181
TrEMBL
Secretory Pathway (Reliability: 2)
H7C012_HUMAN
510
0
56641
TrEMBL
Secretory Pathway (Reliability: 4)
G4WMG7_HUMAN
504
1
55257
TrEMBL
Secretory Pathway (Reliability: 4)
A8K1Z7_HUMAN
498
0
55766
TrEMBL
Secretory Pathway (Reliability: 1)
A6H8L5_HUMAN
499
0
55556
TrEMBL
Secretory Pathway (Reliability: 1)
E7EX42_HUMAN
118
0
13373
TrEMBL
Secretory Pathway (Reliability: 2)
E7EUJ1_HUMAN
499
0
55617
TrEMBL
Secretory Pathway (Reliability: 1)
L7NSP5_HUMAN
504
1
55330
TrEMBL
Secretory Pathway (Reliability: 4)
E7EUK6_HUMAN
438
0
49026
TrEMBL
Secretory Pathway (Reliability: 1)
LIPR1_HUMAN
467
0
51848
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
-
colipase
32000
-
x * 47000, wild-type enzyme, SDS-PAGE, x * 43000, lid domain lacking mutant, SDS-PAGE, x * 32000, cap domain lacking mutant, SDS-PAGE
43000
-
x * 47000, wild-type enzyme, SDS-PAGE, x * 43000, lid domain lacking mutant, SDS-PAGE, x * 32000, cap domain lacking mutant, SDS-PAGE
47000
-
x * 47000, wild-type enzyme, SDS-PAGE, x * 43000, lid domain lacking mutant, SDS-PAGE, x * 32000, cap domain lacking mutant, SDS-PAGE
48000
-
x * 48000, SDS-PAGE
49946
-
x * 50000, recombinant enzyme, SDS-PAGE, x * 52343, recombinant glycosylated enzyme, mass spectrometry, x * 49946, recombinant nonglycosylated enzyme, mass spectrometry
50000
52343
-
x * 50000, recombinant enzyme, SDS-PAGE, x * 52343, recombinant glycosylated enzyme, mass spectrometry, x * 49946, recombinant nonglycosylated enzyme, mass spectrometry
67000
-
x * 67000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
side-chain modification
-
contains approximately 8% carbohydrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E250Q
-
site-directed mutagenesis, the mutant shows reduced triacylglyceride lipase activity compared to the wild-type endothelial lipase
FS270
-
mutant exhibits increased activity (2.0fold more active compared to the wild type enzyme)
FS282
-
mutant exhibits increased activity (7.6fold more active compared to the wild type enzyme)
G241R
-
site-directed mutagenesis, the mutant shows reduced triacylglyceride lipase activity compared to the wild-type endothelial lipase
H151A
-
mutant shows changed pH-activity profile and reduced lipase activity compared to the wild type enzyme
I408D
-
site-directed mutagenesis, reduced activity, altered substrate specificity, and increased lag time compared to the wild-typ enzyme, water-accessible surface area of the beta5'-loop compared to the wild-type enzyme's loop
I408K
-
site-directed mutagenesis, reduced activity, altered substrate specificity, and increased lag time compared to the wild-typ enzyme, water-accessible surface area of the beta5'-loop compared to the wild-type enzyme's loop
K80E
-
mutant shows changed pH-activity profile and reduced lipase activity compared to the wild type enzyme
L264E
-
mutant shows changed pH-activity profile and reduced lipase activity compared to the wild type enzyme
L412D
-
site-directed mutagenesis, slightly reduced activity compared to the wild-typ enzyme, water-accessible surface area of the beta5'-loop compared to the wild-type enzyme's loop
L412K
-
site-directed mutagenesis, slightly reduced activity compared to the wild-typ enzyme, water-accessible surface area of the beta5'-loop compared to the wild-type enzyme's loop
N79Q
-
site-directed mutagenesis, disruption of N-glycosylation site, the N-glycosylation at Asn70 is not required for activity
P195L
-
the mutant exhibits reduced activity and is associated with neutral lipid storage disease that is characterized by systemic triglycerol accumulation and myopathy
Q289X
-
mutant exhibits increased activity (24.6fold more active compared to the wild type enzyme)
S152G
-
inactive mutant, the inactive enzyme mutant S152G binds to tricaprylin in a water emulsion interface competiting with the active enzyme hydrolyzing the substrate, overview
T372A
-
the mutation gives a protein that binds lipid droplets and functions the same as the wild type protein
V407D
-
site-directed mutagenesis, reduced activity, altered substrate specificity, and increased lag time compared to the wild-typ enzyme, water-accessible surface area of the beta5'-loop compared to the wild-type enzyme's loop
V407K
-
site-directed mutagenesis, reduced activity, altered substrate specificity, and increased lag time compared to the wild-typ enzyme, water-accessible surface area of the beta5'-loop compared to the wild-type enzyme's loop
Y114F
-
mutant shows changed pH-activity profile and reduced lipase activity compared to the wild type enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from liver microsomes
-
heparin-Sepharose column chromatography
-
recombinant from Sf9 insect cells, about 30fold
-
recombinant secreted enzyme from protease A-deficient Pichia pastoris strain culture supernatant by cation and anion exchange chromatography to homogeneity
-
recombinant wild-type and mutant enzymes from insect cells, mutant lacking the cap domain is only stable at acidic pH value during purification
-
recombinant wild-type and mutant enzymes from Pichia pastoris
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli M15 with a N-terminal His-tagged substituting the signal sequence, the expressed protein is insoluble and inactive, expression of the C-terminally His-tagged enzyme containing its native signal sequence in Spodoptera frugiperda Sf9 insect cells via baculovirus infection results in active enzyme
-
expressed in COS-7 cells
-
expressed in Pichia pastoris
-
expressed in Pichia pastoris strain GS115 and Sf21 insect cells
-
expression in Pichia pastoris, best expression is obtained by replacing the native signal peptide with a yeast signal peptide
-
expression of PLRP2 in the protease A-deficient yeast Pichia pastoris as secreted enzyme
-
expression of wild-type and mutant enzymes in Pichia pastoris
-
expression of wild-type enzyme and mutants lacking the cap and the lid domain via baculovirus transfection in insect cells
-
functional expression of wild-type and C-terminally truncated or non-glycosylated secreted mutant enzymes in RH-17777 cells
-
the genes encoding the enzyme are located on chromosome 16 within a cluster of carboxylesterase genes, genetic organization, expression analysis
-
the HSL gene is located on chromosome 19q13.2. The ATGL gene PNPLA2 span 6.32 kb of genomic DNA, which are located on chromosome 11p15.5
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mRNA and protein levels are reduced in obese patients with insulin resistance
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Augustin, J.; Freeze, H.; Tejada, P.; Brown, W.V.
A comparison of molecular properties of hepatic triglyceride lipase and lipoprotein lipase from human post-heparin plasma
J. Biol. Chem.
253
2912-2920
1978
Homo sapiens
Manually annotated by BRENDA team
Busch, S.J.; Barnhart, R.L.; Martin, G.A.; Flanagan, M.A.; Jackson, R.L.
Differential regulation of hepatic triglyceride lipase and 3-hydroxy-3-methylglutaryl-CoA reductase gene expression in a human hepatoma cell line, HepG2
J. Biol. Chem.
265
22474-22479
1990
Homo sapiens
Manually annotated by BRENDA team
Dichek, H.L.; Parrott, C.; Ronan, R.; Brunzell, J.D.; Brewer, H.B.; Santamarina-Fojo, S.
Functional characterization of a chimeric lipase genetically engineered from human lipoprotein lipase and human hepatic lipase
J. Lipid Res.
34
1393-1401
1993
Homo sapiens
Manually annotated by BRENDA team
Waterman, I.J.; Emmison, N.; Dutta-Roy, A.K.
Characterisation of triacylglycerol hydrolase activities in human placenta
Biochim. Biophys. Acta
1394
169-174
1998
Homo sapiens
Manually annotated by BRENDA team
Yang, Y.; Lowe, M.E.
Human pancreatic triglyceride lipase expressed in yeast cells: purification and characterization
Protein Expr. Purif.
13
36-40
1998
Homo sapiens
Manually annotated by BRENDA team
Lowe, M.E.
Colipase stabilizes the lid domain of pancreatic triglyceride lipase
J. Biol. Chem.
272
9-12
1997
Homo sapiens
Manually annotated by BRENDA team
Miled, N.; Bussetta, C.; De Caro, A.; Riviere, M.; Berti, L.; Canaan, S.
Importance of the lid and cap domains for the catalytic activity of gastric lipases
Comp. Biochem. Physiol. B
136B
131-138
2003
Homo sapiens
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Carriere, F.; Renou, C.; Lopez, V.; De Caro, J.; Ferrato, F.; Lengsfeld, H.; De Caro, A.; Laugier, R.; Verger, R.
The specific activities of human digestive lipases measured from the in vivo and in vitro lipolysis of test meals
Gastroenterology
119
949-960
2000
Homo sapiens
Manually annotated by BRENDA team
Alam, M.; Ho, S.; Vance, D.E.; Lehner, R.
Heterologous expression, purification, and characterization of human triacylglycerol hydrolase
Protein Expr. Purif.
24
33-42
2002
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kobayashi, J.; Kusunoki, M.; Murase, Y.; Kawashiri, M.; Higashikata, T.; Miwa, K.; Katsuda, S.; Takata, M.; Asano, A.; Nohara, A.; Inazu, A.; Mabuchi, H.
Relationship of lipoprotein lipase and hepatic triacylglycerol lipase activity to serum adiponectin levels in Japanese hyperlipidemic men
Horm. Metab. Res.
37
505-509
2005
Homo sapiens
Manually annotated by BRENDA team
Jenkins, C.M.; Mancuso, D.J.; Yan, W.; Sims, H.F.; Gibson, B.; Gross, R.W.
Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities
J. Biol. Chem.
279
48968-48975
2004
Homo sapiens
Manually annotated by BRENDA team
Freie, A.B.; Ferrato, F.; Carriere, F.; Lowe, M.E.
Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles
J. Biol. Chem.
281
7793-7800
2006
Homo sapiens
Manually annotated by BRENDA team
Gilham, D.; Alam, M.; Gao, W.; Vance, D.E.; Lehner, R.
Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates
Mol. Biol. Cell
16
984-996
2005
Homo sapiens
Manually annotated by BRENDA team
Yamada, M.; Fujita, T.
New procedure for the measurement of pancreatic lipase activity in human serum using a thioester substrate
Clin. Chim. Acta
383
85-90
2007
Homo sapiens
Manually annotated by BRENDA team
Jocken, J.W.; Smit, E.; Goossens, G.H.; Essers, Y.P.; van Baak, M.A.; Mensink, M.; Saris, W.H.; Blaak, E.E.
Adipose triglyceride lipase (ATGL) expression in human skeletal muscle is type I (oxidative) fiber specific
Histochem. Cell Biol.
129
535-538
2008
Homo sapiens
Manually annotated by BRENDA team
Griffon, N.; Budreck, E.C.; Long, C.J.; Broedl, U.C.; Marchadier, D.H.; Glick, J.M.; Rader, D.J.
Substrate specificity of lipoprotein lipase and endothelial lipase: studies of lid chimeras
J. Lipid Res.
47
1803-1811
2006
Homo sapiens
Manually annotated by BRENDA team
Eydoux, C.; De Caro, J.; Ferrato, F.; Boullanger, P.; Lafont, D.; Laugier, R.; Carriere, F.; De Caro, A.
Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells
J. Lipid Res.
48
1539-1549
2007
Homo sapiens
Manually annotated by BRENDA team
Colin, D.Y.; Deprez-Beauclair, P.; Allouche, M.; Brasseur, R.; Kerfelec, B.
Exploring the active site cavity of human pancreatic lipase
Biochem. Biophys. Res. Commun.
370
394-398
2008
Homo sapiens
Manually annotated by BRENDA team
Schweiger, M.; Schoiswohl, G.; Lass, A.; Radner, F.P.; Haemmerle, G.; Malli, R.; Graier, W.; Cornaciu, I.; Oberer, M.; Salvayre, R.; Fischer, J.; Zechner, R.; Zimmermann, R.
The C-terminal region of human adipose triglyceride lipase affects enzyme activity and lipid droplet binding
J. Biol. Chem.
283
17211-17220
2008
Homo sapiens
Manually annotated by BRENDA team
Imamura, S.; Kobayashi, J.; Nakajima, K.; Sakasegawa, S.; Nohara, A.; Noguchi, T.; Kawashiri, M.A.; Inazu, A.; Deeb, S.S.; Mabuchi, H.; Brunzell, J.D.
A novel method for measuring human lipoprotein lipase and hepatic lipase activities in postheparin plasma
J. Lipid Res.
49
1431-1437
2008
Homo sapiens
Manually annotated by BRENDA team
Watt, M.J.
Triglyceride lipases alter fuel metabolism and mitochondrial gene expression
Appl. Physiol. Nutr. Metab.
34
340-347
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chatterjee, C.; Young, E.K.; Pussegoda, K.A.; Twomey, E.E.; Pandey, N.R.; Sparks, D.L.
Hepatic high-density lipoprotein secretion regulates the mobilization of cell-surface hepatic lipase
Biochemistry
48
5994-6001
2009
Homo sapiens
Manually annotated by BRENDA team
Zimmermann, R.; Lass, A.; Haemmerle, G.; Zechner, R.
Fate of fat: the role of adipose triglyceride lipase in lipolysis
Biochim. Biophys. Acta
1791
494-500
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Zechner, R.; Kienesberger, P.C.; Haemmerle, G.; Zimmermann, R.; Lass, A.
Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores
J. Lipid Res.
50
3-21
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Rouhani, N.; Young, E.; Chatterjee, C.; Sparks, D.L.
HDL composition regulates displacement of cell surface-bound hepatic lipase
Lipids
43
793-804
2008
Homo sapiens
Manually annotated by BRENDA team
Xie, X.; Langlais, P.; Zhang, X.; Heckmann, B.L.; Saarinen, A.M.; Mandarino, L.J.; Liu, J.
Identification of a novel phosphorylation site in adipose triglyceride lipase as a regulator of lipid droplet localization
Am. J. Physiol. Endocrinol. Metab.
306
E1449-E1459
2014
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chen, K.Y.; Chang, S.S.; Chen, C.Y.
In silico identification of potent pancreatic triacylglycerol lipase inhibitors from traditional Chinese medicine
PLoS ONE
7
e43932
2012
Homo sapiens (P16233), Homo sapiens
Manually annotated by BRENDA team