Information on EC 3.1.1.34 - lipoprotein lipase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.1.34
-
RECOMMENDED NAME
GeneOntology No.
lipoprotein lipase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycerolipid metabolism
-
-
triacylglycerol degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
triacylglycero-protein acylhydrolase
Hydrolyses triacylglycerols in chylomicrons and low-density lipoproteins. Also hydrolyses diacylglycerol.
CAS REGISTRY NUMBER
COMMENTARY hide
9004-02-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
European sea bass
Uniprot
Manually annotated by BRENDA team
Mus musculus C57BL/6J
C57BL/6J mice
-
-
Manually annotated by BRENDA team
strain ICR
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
KY 521
-
-
Manually annotated by BRENDA team
KY 521
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-ditetradecyl-3[9(1-pyrenyl)nonanoyl]glyceride + H2O
?
show the reaction diagram
-
-
-
-
?
1,2-O-dilauryl-DL-glycero-3-glutaric acid-(6-methylresorufin ester) + H2O
?
show the reaction diagram
1,2-O-dilauryl-rac-glycero-3-glutaric acid-(6'-methylresorufin) ester + H2O
?
show the reaction diagram
-
-
-
-
?
1,3-dioleoyl-2[4(1-pyrenyl)butanoyl]glycerol + H2O
?
show the reaction diagram
-
-
-
-
?
1-lauryl-2[9(1-pyrenyl) nonanoyl]phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine + H2O
myristic acid + 2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine
show the reaction diagram
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-
-
?
1-myristoyl-2[9(1-pyrenyl)nonanoyl]diglyceride + H2O
?
show the reaction diagram
-
-
-
-
?
1-myristoyl-2[9(1-pyrenyl)nonanoyl]phosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
1-myristoyl-2[9(1-pyrenyl)nonanoyl]phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
1-myristoyl-2[9(1pyrenyl)nonaoyl]phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
chylomicron + H2O
?
show the reaction diagram
chylomicrons + H2O
?
show the reaction diagram
EnzChek lipase substrate + H2O
?
show the reaction diagram
L-alpha-dimyristoylphosphatidylcholine + H2O
?
show the reaction diagram
-
necessity of a lipid bilayer structure
-
-
?
low-density lipoprotein + H2O
?
show the reaction diagram
-
low activity
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyric acid
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
?
triacetin + H2O
acetate + diacetin
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
tributyrin + H2O
?
show the reaction diagram
tributyrin + H2O
butanoate + dibutyrin
show the reaction diagram
-
-
-
?
tricaprin + H2O
?
show the reaction diagram
tricaproin + H2O
?
show the reaction diagram
tricaprylin + H2O
?
show the reaction diagram
tricaprylin + H2O
capric acid + dicaprylin
show the reaction diagram
-
-
-
?
trioctanoin + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
triolein + H2O
dioleylglycerol + oleate
show the reaction diagram
-
mutant D204 E, very low activity in presence of emulsifier Triton X-100 or phosphatidylcholine. In presence of phosphatidylethenolamine, phospatidylserine, and cardiolipin as emulsifier, triolein-hydrolizing activity of the mutant is higher than wild-type activity
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
tripropionin + H2O
propionate + dipropionin
show the reaction diagram
-
-
-
?
very low density lipoprotein + H2O
?
show the reaction diagram
very low density lipoprotein + H2O
esterified oxylipins
show the reaction diagram
-
-
-
-
?
very low density lipoprotein + H2O
intermediate density lipoprotein + ?
show the reaction diagram
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-
-
-
?
very low density protein + H2O
?
show the reaction diagram
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-
-
-
?
very-low-density lipoprotein + H2O
?
show the reaction diagram
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-
-
-
?
very-low-density lipoproteins + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
very low density lipoprotein + H2O
intermediate density lipoprotein + ?
show the reaction diagram
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-
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
apolipoprotein CII
-
important cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
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0.01-0.015 mM, almost complete inhibition of tributyrin and tripropionin hydrolysis, competes for binding with apoprotein CII, inhibition is prevented or restored by apoprotein CII
2-mercaptoethanol
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3-[4'-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)biphenyl-3-yl]propanoic acid
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4-ethylphenylboronic acid
-
-
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4-nonylphenylboronic acid
-
-
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4-tert-butyl-N-[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)phenyl]benzamide
-
-
5,5'-dithiobis(2-nitrobenzoate)
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-
angiopoietin-like protein 3
angiopoietin-like protein 4
angiopoietin-like protein-4
ANGPTL4
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conventional, non-competitive inhibitor
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antiserum
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produced in goat
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antiserum to rat adipose tissue lipoprotein lipase
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-
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Apo AI
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0.001 mM, 25% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
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Apo AII
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0.001 mM, 50% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
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Apo CI
-
0.0005 mM, 72% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
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apolipoprotein A I
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apolipoprotein A II
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apolipoprotein C I
apolipoprotein C III
apolipoprotein E
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apolipoprotein-Ala
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apolipoprotein-Ser
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apoliprotein A I
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catechin
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catechin shows 43.6% inhibitory effect at 0.2 mg/ml
cytochalasin D
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preincubation with cytochalasin D prevents the increase in dexmethasone-induced lipoprotein lipase activity
diisopropyl fluorophosphate
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dithiothreitol
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dodecanesulfonyl fluoride
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0.01 mM-0.02 mM, 50% inhibition, complete inhibition after 24 h
fragments of apolipoprotein E
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-
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heat-inactivated rat serum
hexadecanesulfonyl fluoride
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0.01 mM-0.02 mM, 50% inhibition, complete inhibition after 24 h
hexanesulfonyl fluoride
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almost complete inhibition after 24 h
HgCl2
-
-
LG268
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retinoid X receptor selective retinoid, almost complete inactivation of LPL activity in heart muscle after administration of 30 mg/kg/d, approx. 50% inhibition in skeletal muscle
Lys-Gly-Glu-Glu
N-[3-aminopropyl-[4-(3-aminopropylamino)butyl]amino]-N-hydroxynitrous amide
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i.e. spermine NONOate, tissue LPL activity tends to decrease 5 min after the addition of 0.1 mM spermine NONOate
P-407
-
-
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p-hydroxymercuribenzoate
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phenylmethylsulfonyl fluoride
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protamine
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Protamine sulfate
reduced glutathione
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RHC-80267
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i.e. 1,6-di(O-(carbamoyl)cyclohexanone oxime)hexane, is a highly selective DAGL inhibitor. It significantly reduces L- and N-current inhibition by the muscarinic agonist oxotremorine-M, Oxo-M, but does not affect their inhibition by exogenous arachidonic acid, currents by Ba2+ or Ca2+. Moreover, voltage-dependent inhibition of N-current by Oxo-M remains in the presence of RHC-80267, indicating selective action on the slow pathway, i.e. the voltage-independent, pertussis-toxin insensitive pathway. RHC-80267 also blocks inhibition of recombinant N-current, but has no effect on native M-current inhibition
Sodium deoxycholate
tetrahydrolipstatin
Triton WR-1339
Tween 20
-
96.38% relative activity in the presence of 1% (v/v) Tween 20
Tween 40
-
86.0% relative activity in the presence of 5% (v/v) Tween 40
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
angiopoietin-like protein 4
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major physiological regulator of enzyme activity under conditions of fasting and exercise
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apoC-II
apoCII
apolipoprotein A5
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-
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apolipoprotein C-II
apolipoprotein-Glu
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activates
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apoprotein C II
apoprotein CII
calnexin
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promotes formation of active LPL dimers
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calreticulin
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promotes formation of active LPL dimers
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dexamethasone
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induces increase in coronary lipoprotein lipase, combination of 100 nM dexmethasone with 100 nM insulin appreciably enhances lipoprotein lipase activity
glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1
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binds lipoprotein lipase and chylomicrons and is a platform for lipolysis within capillaries
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Gum arabic
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197.6% relative activity in the presence of 1% (w/v) Gum Arabic, emulsifier for determination of LPL activity
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heparin
high-density lipoprotein
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stimulation
-
human apoCII
0.002 mg/ml, approx. 9fold activation
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Insulin
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combination of 100 nM dexmethasone with 100 nM insulin appreciably enhances lipoprotein lipase activity
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plasma
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from trout, stimulates
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Tween 80
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409.6% relative activity in the presence of 5% (v/v) Tween 80
very-low-density lipoprotein
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strong stimulation
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.12 - 1.77
chylomicron
0.075 - 0.083
chylomicrons
-
soluble enzyme
-
0.0002 - 1.57
triolein
2.5
trioleoin
-
-
-
0.97 - 1.68
very-low-density lipoprotein
0.026 - 0.053
Very-low-density lipoproteins
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00004 - 0.0047
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
3-[4'-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)biphenyl-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
4-ethylphenylboronic acid
Homo sapiens
-
pH and temperature not specified in the publication
-
0.0014
4-nonylphenylboronic acid
Homo sapiens
-
pH and temperature not specified in the publication
-
0.0002
4-tert-butyl-N-[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.7
-
substrate tributyrin
39.2
-
substrate triolein
47.75
-
-
56.95
-
-
333.3
-
-
431.6
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
-
hydrolysis of triolein
9
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(3-[1,1-dimethyl-2-hydroxyethyl]amino)-2-hydroxypropane-sulfonic acid buffer
9.4
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glycine buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 8.9
-
pH 7.2: about 45% of maximal activity, pH 8.9: about 95% of maximal activity
7.5 - 9.8
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pH 7.5: about 80% of maximal activity, pH 9.8: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
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20C: about 35% of maximal activity, 40C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.6
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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limb muscle, increase of enzyme activity and mRNA level upon chronic stress
Manually annotated by BRENDA team
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GPIHBP1 shuttles lipoprotein lipase from subendothelial spaces to the capillary lumen
Manually annotated by BRENDA team
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noncancer tissue. Lipoprotein lipase activity is higher in cancer tissue than in noncancer tissue. Lipoprotein lipase gene expression is higher in noncancer tissue compared to cancer tissue
Manually annotated by BRENDA team
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SCG neurons
Manually annotated by BRENDA team
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transgenic animals with beta-cell-specific overexpression or inactivation of enzyme. Enzyme activity and triglyceride content is increased in overexpressing islets, decreased enzyme activity enzyme-inactivated islets does not affect islets triglyceride content. Both overexpressing and enzyme-inactivited mice are strikingly hyperglycemic during glucose tolerance testing, and both show impaired glucose-simulated insulin secretion
Manually annotated by BRENDA team
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LPL is synthesized by parenchymal cells, from which it is secreted and then transported to the lumen surface of endothelial cells
Manually annotated by BRENDA team
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fasting for 2 weeks or insulin administration has no effect on activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
-
gel filtration
64000
-
gel filtratiion
67000
-
gel filtration
75000
-
gel filtration
100000 - 110000
-
gel filtration
121000
-
gel filtration
123000
-
gel filtration
additional information
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-
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
side-chain modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
45C, 15 min, 70% loss of activity
80900
5
-
45C, 15 min, stable
80900
6.5
-
rapid inactivation below
80908
7
-
45C, 15 min, 10% loss of activity
80900
8.5
-
rapid inactivation above
80908
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18
-
5 mM sodium barbital buffer, pH 7.5, 20% v/v glycerol, 0.1% v/v Triton X-100, 2 M NaCl, half-life: 40 h
40
-
20 min, 50% loss of activity
50
-
pH 5-7, 15 min, stable up to
additional information
-
high concentrations of glycerol or glycine prevent inactivation at 37C and at 4C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme has a strong propensity to aggregate. No aggregation is observed at 0.3 M NaCl concentration or higher. Albumin or heparin may prevent aggregation at 0.15 M NaCl
-
heparin has a limited role in stabilizing the bound LPL active dimers
-
high concentrations of NaCl increase the rate of inactivation
-
the partially purified enzyme at later stages is stabilized by the inclusion of 20% glycerol in the buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 1 mg bovine serum albumin per ml or 50% glycerol, stable for several days
-
-70C, 8 weeks, 20% loss of activity
-
0C, 1% serum albumin, 1 h, 60% loss of activity
-
4C, moderate stability
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
biotinylated enzyme by sucrose density gradient centrifugation and heparin affinity chromatography
-
heparin affinity chromatography
-
heparin-Sepharose, partially purified
partial
partially purified by heparin-Sepharose column chromatography
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partially purified using heparin-Sepharose affinity column chromatography
-
recombinant enzyme is purified by TALON metal affinity resin chromatography
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recombinant LPL
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sedimentation in 10 mM sodium sulfite followed by centrifugation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chimeric lipase consisting of the amino-terminal 314 amino acids of human lipoprotein lipase and the carboxyl-terminal 146 amino acids of human hepatic lipase
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expressed in Escherichia coli
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expressed in HEK-293 cells
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expressed in J-774 cells
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expressed in Mus musculus
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expressed in Mus musculus mammary glands (milk)
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expression in COS cells
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expression in HEK 293 cells
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expression in HHO cells
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expression in rabbit inhibits diet-induced hypercholesterolemia and atherosclerosis
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expression in Sf21 insect cells, coexpression with calreticulin enhances yield of active LPL by a factor 9
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expression of LPL mini gene in mice
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fusion protein consisting of the complete lipoprotein lipase molecule and the mature form of apolipoprotein CII, expression in human embryonic kidney 293 cells
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LPL overexpression in Mus musculus skeletal muscle increases cold tolerance by enhancing capacity for fat oxidation, producing an avian-like phenotype in which skeletal muscle contributes significantly to the thermogenic response to cold temperatures
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during embryogenesis, the mRNA level is increased gradually
insulin, dexamethasone and cortisol increase mRNA and activity in adipose organs. Cold markedly stimulates enzyme activity in brown adipose tissue
-
interferon mediates inhibition of lipoprotein lipase gene transcription in macrophages, the mechanism involves a reduction in the binding of transcription factors Sp1 and Sp3 to regulatory sequences in the LPL gene with casein kinase 2- and phosphoinositide-3-kinase-mediated regulation of transcription factors Sp1 and Sp3, overview
lipoprotein lipase activity is significantly decreased in the ischemic side cortex at 2 h ischemia
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skeletal muscle lipoprotein lipase activity is increased in leptin-treated (2 mg/kg body weight over 2 weeks) compared with pair-fed and wild type mice
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stress and catecholamines reduce adipose enzyme activity. Tissue necrosis factpor alpha represses enzyme activity by downregulating transcription
-
the mRNA expression and activity of brain lipoprotein lipase (LPL) is increased after acute cerebral ischemia-reperfusion in rats. Increase of LPL immunopositive cells in the cerebral cortex around the infarction area is observed at 4, 6, 12 h ischemia, 2 h ischemia 2 h reperfusion, and 4 h ischemia 2 h reperfusion
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there is no effect of leptin treatment (2 mg/kg body weight over 2 weeks) or pair feeding on postprandial adipose tissue lipoprotein lipase activity
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W114A
-
completely inactive lipase
W390A
-
decreased activity with monoclonal antibody 5D2, decreased activity against a synthetic emulsion of long-chain triacylglycerols and in particular against rat lymph chylomicrons
W55A
-
completely inactive lipase
C418Y
-
the mutation abolishes lipoprotein lipases's ability to bind to GPIHBP1 and therefore abolishes LPL transport across endothelial cells byGPIHBP1, without interfering with the enzyme catalytic activity or binding to heparin
D204E
-
homozygous missense mutation identified in a patient with severe hypertriglyceridemia, post-heparin enzyme mass is almost normal, but the enzyme activity is remarkably decreased. In presence of phosphatidylethenolamine, phospatidylserine, and cardiolipin as emulsifier, triolein-hydrolizing activity of the mutant is higher than wild-type activity
D9N
-
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease
E421K
-
the mutation abolishes lipoprotein lipases's ability to bind to GPIHBP1 and therefore abolishes LPL transport across endothelial cells byGPIHBP1, without interfering with the enzyme catalytic activity or binding to heparin
K430A/R432A/K434A/K440A/K441A
-
the mutant LPL has little or no ability to bind to GPIHBP1 on the surface of cells
N291S
-
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
after fulll denaturation in 6 M guanidinium choride or after dissociation in monomers in 1 M guanidinium chloride. Presence of Ca2+ is crucial for reactivation, which involves at least two steps. First step is rapid and results in formation of an inactive monomer with a completely folded C-terminal domain, second step is promoted by Ca2+ and converts enzyme monomers to dimerization-competent and more tightly folded monomers that rapidly form active dimers. Proline isomerization is rate-limiting for the second step
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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