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
3.1.1.34
-
RECOMMENDED NAME
GeneOntology No.
lipoprotein lipase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
clearing factor
-
-
-
-
DAG lipase
-
-
diacylglycerol hydrolase
-
-
-
-
diacylglycerol lipase
-
-
-
-
diacylglycerol lipase
-
-
diglyceride lipase
-
-
-
-
heparin-releasable protein lipase
-
-
lipemia-clearing factor
-
-
-
-
LIPL
-
-
lipoprotein lipase
P06858
-
LPL
-
-
-
-
LPL
P11151
-
LPL
Q6P2U2
-
LPL
P06858
-
LPL
Mus musculus C57BL/6J, Mus musculus ICR
-
-
-
postheparin esterase
-
-
-
-
postheparin lipase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9004-02-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
induction of endogenous enzyme production by dexamethasone
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
wild-type enzyme and mutant enzymes W382A, W390A, W393A, W394A, W393A/W394A and W114A
-
-
Manually annotated by BRENDA team
European sea bass
Uniprot
Manually annotated by BRENDA team
expression in transgenic rabbit
-
-
Manually annotated by BRENDA team
functional deficiency of enzyme in a patient with severe hypertriglyceridemia
-
-
Manually annotated by BRENDA team
healthy males
-
-
Manually annotated by BRENDA team
Japanese hyperlipidemic men
-
-
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
male C57BL/6 mice
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
retinoid X receptor gamma-deficient mice, increase in activity of skeletal enzyme isoform
-
-
Manually annotated by BRENDA team
strain ICR
-
-
Manually annotated by BRENDA team
transgenic animals with beta-cell-specific overexpression or inactivation of enzyme
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
C57BL/6J mice
-
-
Manually annotated by BRENDA team
Mus musculus ICR
strain ICR
-
-
Manually annotated by BRENDA team
Richardson
-
-
Manually annotated by BRENDA team
adult male Sprague-Dawley and Wistar rats
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
Rhizopus japonicus KY 521
KY 521
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
lipoprotein lipase knock-out mice die 18 h after birth, probably because of hypoglycemia
malfunction
-
selective loss of adipocyte enzyme in mice leads to mild hypertriglyceridemia. Enzyme-deficient mice display a profound increase in de novo lipogenesis-fatty acids, especially palmitoleate and myristoleate in brown adipose tissue and white adipose tissue depots while essential dietary fatty acids are markedly decreased. High fat diet-fed enzyme-deficient mice exhibit less adiposity and improved plasma adipokines but not increased glucose tolerance
metabolism
-
the phosphoinositide-3-kinase pathway is involved in the regulation of LPL gene transcription through Sp1/Sp3, signalling pathways that impact on the IFN-mediated regulation of Sp1/Sp3 binding and LPL gene transcription in macrophages, overview. The synergism between IFN- and TNF- on LPL gene transcription is not mediated at the level of Sp1/Sp3 DNA binding
metabolism
-
lipoprotein lipase is a major enzyme in lipid metabolism responsible for the hydrolysis of the core triglycerides in chylomicrons and very low density lipoprotein and subsequent release of free fatty acids
physiological function
-
arachidonic acid signaling requires DAGL in many systems. L- and N-current but not M-current inhibition by M1 muscarinic receptors requires DAG lipase activity, overview. The signaling pathway mediating L- and N-current inhibition diverges from the pathway initiating M-current inhibition
physiological function
-
lipoprotein lipase is a principal enzyme responsible for the clearance of chylomicrons and very low density lipoproteins from the bloodstream. The activity of LPL is tightly modulated by multiple mechanisms in a tissue-specific manner in response to nutritional changes
physiological function
-
lipoprotein lipase (LPL) reduces the infectivity of hepatitis C virus through its catalytic activity on hepatitis C virus-associated lipoproteins. LPL treatment reduces association of hepatitis C virus with ApoE
physiological function
-
lipoprotein lipase is an amyloid beta-binding protein that promotes glycosaminoglycan-dependent cellular uptake of amyloid beta in astrocytes
physiological function
-
lipoprotein lipase LPL expressed in placenta facilitates uptake of retinoids by this organ and their transfer to the embryo, mainly through its catalytic activity. In addition, LPL can mediate the acquisition of nascent chylomicrons by the placenta, although less efficiently. Placental LPL acts in concert with low density lipoprotein receptor and LRP1
physiological function
-
lipoprotein lipase plays a potential role in the pathophysiological response of the brain to cerebral ischemia-reperfusion
physiological function
-
lipoprotein lipase serves a dual function as a triglyceride lipase of circulating chylomicrons and very-low-density lipoproteins and facilitates receptor-mediated lipoprotein uptake into heart, muscle and adipose tissue
physiological function
-
overexpression of human lipoprotein lipase in mouse mammary glands leads to reduction of milk triglyceride and delayed growth of suckling pups
physiological function
-
the enzyme is rate limiting for plasma triglyceride clearance and tissue uptake of fatty acids
physiological function
-
the up-regulation of enzyme activity may be beneficial in obesity and diabetes
physiological function
Mus musculus C57BL/6J
-
lipoprotein lipase is a principal enzyme responsible for the clearance of chylomicrons and very low density lipoproteins from the bloodstream. The activity of LPL is tightly modulated by multiple mechanisms in a tissue-specific manner in response to nutritional changes
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
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
-
-
-
-
?
chylomicron + H2O
?
show the reaction diagram
-
-
-
-
?
chylomicron + H2O
?
show the reaction diagram
Mus musculus ICR
-
-
-
-
?
chylomicrons + H2O
?
show the reaction diagram
-
-
-
-
?
chylomicrons + H2O
?
show the reaction diagram
-
-
-
-
?
chylomicrons + H2O
?
show the reaction diagram
-
-
-
-
?
chylomicrons + H2O
?
show the reaction diagram
-
-
-
-
?
chylomicrons + H2O
?
show the reaction diagram
-
wild-type enzyme and mutant enzymes
-
-
?
EnzChek lipase substrate + H2O
?
show the reaction diagram
-
a commercially available BODIPY, Dabcyl-labeled triglyceride analog substrate, C58H85BF2N6O6
-
-
?
L-alpha-dimyristoylphosphatidylcholine + H2O
?
show the reaction diagram
-
necessity of a lipid bilayer structure
-
-
?
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
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
Q9W6Y2
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
catalyzes the hydrolysis of triglycerides in circulating chylomicrons and very-low density lipoproteins
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
wild-type enzyme and mutant enzymes
-
-
?
tributyrin + H2O
butanoate + dibutyrin
show the reaction diagram
-
-
-
?
tricaprin + H2O
?
show the reaction diagram
Rhizopus japonicus, Rhizopus japonicus KY 521
-
-
-
-
?
tricaproin + H2O
?
show the reaction diagram
Rhizopus japonicus, Rhizopus japonicus KY 521
-
-
-
-
?
tricaprylin + H2O
?
show the reaction diagram
Rhizopus japonicus, Rhizopus japonicus KY 521
-
-
-
-
?
tricaprylin + H2O
capric acid + dicaprylin
show the reaction diagram
-
-
-
?
trioctanoin + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
?
triolein + H2O
?
show the reaction diagram
Rhizopus japonicus, Rhizopus japonicus KY 521
-
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
A4F5E8
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
-
10 mM of triolein with 5% (w/v) bovine serum albumin, 1% (w/v) Gum arabic, and acetonitrile show the optimum conditions for measuring LPL activity
-
-
?
triolein + H2O
oleate + diolein
show the reaction diagram
Mus musculus ICR
-
-
-
-
?
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
-
-
?
tripropionin + H2O
propionate + dipropionin
show the reaction diagram
-
-
-
?
very low density lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
very low density lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
very low density lipoprotein + H2O
?
show the reaction diagram
Mus musculus ICR
-
-
-
-
?
very low density lipoprotein + H2O
esterified oxylipins
show the reaction diagram
-
-
-
-
?
very low density lipoprotein + H2O
intermediate density lipoprotein + ?
show the reaction diagram
-
-
-
-
?
very low density protein + H2O
?
show the reaction diagram
-
-
-
-
?
very-low-density lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
very-low-density lipoproteins + H2O
?
show the reaction diagram
-
-
-
-
?
very-low-density lipoproteins + H2O
?
show the reaction diagram
-
-
-
-
?
very-low-density lipoproteins + H2O
?
show the reaction diagram
-
-
-
-
?
very-low-density lipoproteins + H2O
?
show the reaction diagram
-
-
-
-
?
low-density lipoprotein + H2O
?
show the reaction diagram
-
low activity
-
-
?
additional information
?
-
-
inverse relationship between the hydrolytic rate and the increased acyl-chain unsaturation of monoacid triacylglycerols: C18:1, C18:2, C18:3
-
-
-
additional information
?
-
-
hydrolytic rate of C12 triacylglycerols is higher than C14 triacylglycerols and C16 triacylglycerol
-
-
-
additional information
?
-
-
hydrolysis of saturated monoacid triacylglycerol increases with increase of chain length as C16, C14, C12
-
-
-
additional information
?
-
-
no absolute specificity for monolayers of triglycerides, hydrolysis of diglyceride monolayers at comparable rates
-
-
-
additional information
?
-
-
the enzyme is responsible for the harvesting of fatty acids from the triacylglycerols of circulating serum lipoproteins in those tissues that utilize these triacylglycerols
-
-
-
additional information
?
-
-
the enzyme is rate limiting for the supply of muscle tissue with triglyceride-derived free fatty acids. Improper regulation of the muscle enzyme can lead to major pathogenesis of some human myopathies
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
the obligatory step in the transport of triglyceride fatty acids from circulating chylomicrons and very low density lipoproteins into tissues is hydrolysis of triglyceride core in the lipoprotein particles by lipoprotein lipase
-
-
-
additional information
?
-
-
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
-
additional information
?
-
P11151
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
-
additional information
?
-
P11152
lipoprotein lipase plays a central role in the removal of plasma triglyceride
-
-
-
additional information
?
-
-
lipoprotein lipase hydrolyses the triacylglycerols secreted by the liver and, thus, allows the storage of lipids onto the extrahepatic tissue. Lipoprotein lipase appears to be an important factor for a large or moderate overfeeding induced liver steatosis in different genotypes of ducks
-
-
-
additional information
?
-
-
lipoprotein lipase activity is required for normal cardiac metabolic compensation to hypertensive stress
-
-
-
additional information
?
-
-
the enzyme shows no activity toward cholesterol and high-density lipoprotein
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
Q9W6Y2
-
-
?
very low density lipoprotein + H2O
intermediate density lipoprotein + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is responsible for the harvesting of fatty acids from the triacylglycerols of circulating serum lipoproteins in those tissues that utilize these triacylglycerols
-
-
-
additional information
?
-
-
the enzyme is rate limiting for the supply of muscle tissue with triglyceride-derived free fatty acids. Improper regulation of the muscle enzyme can lead to major pathogenesis of some human myopathies
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
the obligatory step in the transport of triglyceride fatty acids from circulating chylomicrons and very low density lipoproteins into tissues is hydrolysis of triglyceride core in the lipoprotein particles by lipoprotein lipase
-
-
-
additional information
?
-
-
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
-
additional information
?
-
P11151
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
-
additional information
?
-
P11152
lipoprotein lipase plays a central role in the removal of plasma triglyceride
-
-
-
additional information
?
-
-
lipoprotein lipase activity is required for normal cardiac metabolic compensation to hypertensive stress
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
apolipoprotein CII
-
important cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
addition of calcium increases enzyme activity minimally by about 6%
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
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
-
-
3-[4'-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)biphenyl-3-yl]propanoic acid
-
-
4-ethylphenylboronic acid
-
-
-
4-nonylphenylboronic acid
-
-
-
4-tert-butyl-N-[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)phenyl]benzamide
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
angiopoietin-like protein 3
-
mainly exhibits reversible inhibition of the catalytic activity of LPL, heparin is able to overcome the inhibitory effect of angiopoietin-like protein 3 on LPL at a concentration as low as 0.8 units/ml
-
angiopoietin-like protein 3
-
i.e. Angptl3, human, commercial preparation of recombinant enzyme, inhibits LPL activity in vitro and in vivo, structural basis for inhibition, overview. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 46-57 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase
-
angiopoietin-like protein 4
-
heparin is not able to overcome the inhibitory effect of angiopoietin-like protein 4 on LPL at concentrations up to 10 units/ml
-
angiopoietin-like protein 4
-
i.e. Angptl4, human, recombinantly expressed in Escherichia coli. It inhibits LPL activity in vitro and in vivo. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 44-55 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase, involving amino acid residues His46, Gln50, and Gln53, by disrupting the enzyme dimerization, overview. Structural basis for inhibition, overview. Mutants H46A, Q50A, and Q53A are not active against the enzyme
-
angiopoietin-like protein-4
-
-
-
ANGPTL4
-
conventional, non-competitive inhibitor
-
antiserum
-
produced in goat
-
antiserum to rat adipose tissue lipoprotein lipase
-
-
-
Apo AI
-
0.001 mM, 25% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
-
Apo AII
-
0.001 mM, 50% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
-
Apo CI
-
0.0005 mM, 72% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
-
apolipoprotein A I
-
-
-
apolipoprotein A II
-
-
-
apolipoprotein C I
-
-
-
apolipoprotein C I
-
-
-
apolipoprotein C III
-
-
-
apolipoprotein C III
-
-
-
apolipoprotein E
-
-
-
apolipoprotein-Ala
-
-
-
apolipoprotein-Ser
-
-
-
apoliprotein A I
-
-
-
catechin
-
catechin shows 43.6% inhibitory effect at 0.2 mg/ml
cytochalasin D
-
preincubation with cytochalasin D prevents the increase in dexmethasone-induced lipoprotein lipase activity
diisopropyl fluorophosphate
-
-
dithiothreitol
-
-
dodecanesulfonyl fluoride
-
0.01 mM-0.02 mM, 50% inhibition, complete inhibition after 24 h
fragments of apolipoprotein E
-
-
-
heat-inactivated rat serum
-
heat-inactivated rat serum added from 0-10%, decreases the enzyme activity by 12%. HIS also contains lipoprotein lipase-inhibitory factors such as angiopoietin-like protein-3, angiopoietin-like protein-4, apoC-I, and apoC-III
-
hexadecanesulfonyl fluoride
-
0.01 mM-0.02 mM, 50% inhibition, complete inhibition after 24 h
hexanesulfonyl fluoride
-
almost complete inhibition after 24 h
HgCl2
-
-
LG268
-
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
-
-
Lys-Gly-Glu-Glu
-
not only inhibits the basal activity of lipoprotein lipase, but also blocks the activation effect of native apolipoprotein C II
N-[3-aminopropyl-[4-(3-aminopropylamino)butyl]amino]-N-hydroxynitrous amide
-
i.e. spermine NONOate, tissue LPL activity tends to decrease 5 min after the addition of 0.1 mM spermine NONOate
NaCl
-
1 M NaCl inhibits the reaction with triolein by 80%, but there is no inhibition of lipoprotein lipase activity by NaCl if apoC-II is not used in the assay
NaCl
-
1 M NaCl, 90% inhibition
NaCl
-
-
NaCl
-
0.5 M, 80% inhibition, 1 M, 90% inhibition
NaCl
-
1 M, complete inhibition
NaCl
-
-
P-407
-
-
-
p-hydroxymercuribenzoate
-
-
phenylmethylsulfonyl fluoride
-
-
protamine
-
-
Protamine sulfate
-
-
-
Protamine sulfate
-
-
-
Protamine sulfate
-
-
-
Protamine sulfate
-
-
-
reduced glutathione
-
-
RHC-80267
-
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
-
81.8% relative activity in the presence of 5% (w/v) sodium deoxycholate
Sodium deoxycholate
-
-
tetrahydrolipstatin
-
-
tetrahydrolipstatin
-
active-site inhibitor
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
-
LPL activity decreases in the adipose tissue of diabetic rats without significant change in LPL mRNA
-
additional information
-
protein kinase Calpha depletion inhibits LPL translation through protein kinase A activation, LPL translational inhibition occurs through an RNA-binding complex involving protein kinase A subunits and A-kinase-anchoring protein 121, LPL is also translationally repressed following depletion of cellular protein kinase C either through prolonged treatment with phorbol esters or through the use of antisense oligonucleotides to protein kinase Calpha
-
additional information
-
rottlerin, a protein kinase Calpha inhibitor, prevents protein kinase D phosphorylation and the subsequent increase in lipoprotein lipase
-
additional information
-
LPL activity in adipose tissue of rats fed chickpea or lentil flour is 1.7 or 1.5fold lower than that of rats fed casein
-
additional information
-
LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 0.02 mg/ml cyclosporin A for 90 min, LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 20 ng/ml rapamycin for 90 min, LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 20 ng/ml tacrolimus for 90 min, LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 0.01 mg/ml mycophenolate mofetil for 90 min
-
additional information
-
polyaspartate, polyglutamate and a a rabbit antiserum against the acidic domain of glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) block the binding of LPL to GPIHBP1
-
additional information
-
Morinda citrifolia leaf extract shows 66% inhibitory effect at 0.2 mg/ml, Morinda citrifolia fruit extract shows 54.5% inhibitory effect at 0.2 mg/ml, green tea extract shows 54.5% inhibitory effect at 0.2 mg/ml toward lipoprotein lipase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
angiopoietin-like protein 4
-
major physiological regulator of enzyme activity under conditions of fasting and exercise
-
apoC-II
-
apoC-II activates the enzyme 3.5fold in a saturable fashion. Heat-inactivated rat serum is often used as a source of apoC-II for activation of lipoprotein lipase
-
apoCII
-
0.002 mg/ml, 14fold activation
-
apoCII
-
0.002 mg/ml, 25fold activation
-
apolipoprotein A5
-
-
-
apolipoprotein C-II
-
cofactor
-
apolipoprotein C-II
-
-
-
apolipoprotein C-II
-
cofactor; Km: 0.00015 mM
-
apolipoprotein C-II
-
cofactor; Km: 0.001 mM
-
apolipoprotein C-II
-
required
-
apolipoprotein C-II
-
cofactor
-
apolipoprotein C-II
-
-
-
apolipoprotein-Glu
-
activates
-
apoprotein C II
-
requirde for activity, approx. 7fold activation, amino acid residues 65-68 and 73-79 of the LPL N-terminal domain appear to act cooperatively to enable substantial activation
-
apoprotein C II
-
-
-
apoprotein C II
-
-
-
apoprotein CII
-
activation of triolein and phosphatidylcholine hydrolysis in emulsions
-
apoprotein CII
-
100% and 300% of increase in LPL activity for phosphatidyl-choline and triglyceride hydrolysis, respectively
-
calnexin
-
promotes formation of active LPL dimers
-
calreticulin
-
promotes formation of active LPL dimers
-
dexamethasone
-
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
-
binds lipoprotein lipase and chylomicrons and is a platform for lipolysis within capillaries
-
Gum arabic
-
197.6% relative activity in the presence of 1% (w/v) Gum Arabic, emulsifier for determination of LPL activity
-
heparin
-
heparin treatment results in an 11.75fold increase of LPL in the cell culture medium
heparin
-
addition of heparin increases enzyme activity minimally by about 6%
heparin
-
increases hydrolytic activity
heparin
-
weak stimulation
heparin
-
activates
high-density lipoprotein
-
stimulation
-
human apoCII
Q9W6Y2
0.002 mg/ml, approx. 9fold activation
-
NaCl
-
addition of NaCl increases the reaction rate with EnzChek lipase substrate dramatically with the highest rate, 46% higher than that without salt, occurring at 0.15 M
plasma
-
from trout, stimulates
-
Serum
-
stimulates
-
Serum
-
stimulates
-
Tween 80
-
409.6% relative activity in the presence of 5% (v/v) Tween 80
very-low-density lipoprotein
-
strong stimulation
-
Insulin
-
combination of 100 nM dexmethasone with 100 nM insulin appreciably enhances lipoprotein lipase activity
-
additional information
-
2.4 higher LPL activity in patients treated with prednisolone is most probably due to an increase in the active dimeric form of LPL
-
additional information
-
lipoprotein lipase is upregulated at the transcriptional/translational level in patients with mucoskeletal sarcoma
-
additional information
-
glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 represents an important binding site for LPL in vivo
-
additional information
-
oral administration of 120 mg/kg/d body weight of polysaccharides from Auricularia auricula significantly decreases LPL activity in cholesterol-enriched diet-fed mice (the neutral sugars are mainly composed of D-rhamnose, D-xylose, D-glucose and smaller amounts of D-mannose, D-galactose, and D-arabinose)
-
additional information
-
treatment of macrophages with native C-reactive protein increases LPL protein expression and secretion in a dose- and time-dependent manner with maximum stimulatory effect at 0.003 mg/ml, incubation of LPL with vitamin E (0.05 mM) or NAC (10 mM) prevents the stimulatory effect of C-reactive protein on LPL
-
additional information
-
LpL is regulated by feeding/fasting and muscle contraction, insulin stimulates LpL by increasing the level of LpL mRNA and regulating LpL activity through both posttranscriptional and posttranslational mechanisms
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.12
chylomicron
-
-
-
1.77
chylomicron
-
-
-
0.0002
triolein
-
-
0.98
triolein
-
-
1.5
triolein
-
-
1.57
triolein
-
-
2.5
trioleoin
-
-
-
0.97
very-low-density lipoprotein
-
-
-
0.99
very-low-density lipoprotein
-
-
-
1.62
very-low-density lipoprotein
-
-
-
1.68
very-low-density lipoprotein
-
-
-
0.026
Very-low-density lipoproteins
-
enzyme from post-heparin plasma
-
0.053
Very-low-density lipoproteins
-
soluble enzyme
-
0.075 - 0.083
chylomicrons
-
soluble enzyme
-
additional information
additional information
-
Km-values of the chimeric molecule between human lipoprotein lipase and rat hepatic lipase
-
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25C, pH 8.5, hydrolysis of p-nitrophenyl butyrate
0.00028
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25C, pH 8.5, hydrolysis of tripropionin
0.00038
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25C, pH 8.5, hydrolysis of tributyrin
0.0017
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25C, pH 8.5, hydrolysis of tricaprylin
0.0031
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25C, pH 8.5, hydrolysis of triacetin
0.0047
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25C, pH 8.5, hydrolysis of triolein
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
3-[4'-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)biphenyl-3-yl]propanoic acid
-
pH and temperature not specified in the publication
0.02
4-ethylphenylboronic acid
-
pH and temperature not specified in the publication
-
0.0014
4-nonylphenylboronic acid
-
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
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.7
-
substrate tributyrin
39.2
-
substrate triolein
47.75
-
-
56.95
-
-
333.3
-
-
431.6
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
-
hydrolysis of triolein
9
-
(3-[1,1-dimethyl-2-hydroxyethyl]amino)-2-hydroxypropane-sulfonic acid buffer
9.4
-
glycine buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
-
pH 7.5: about 80% of maximal activity, pH 9.8: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
20C: about 35% of maximal activity, 40C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 8.6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
P11152
scopoletin significantly increases lipoprotein lipase activity in 3T3-L1 adipocytes
Manually annotated by BRENDA team
-
preadipocyte cell line
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
preadipocyte cell line
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
-
white adipose tissue
Manually annotated by BRENDA team
Q9W6Y2
highest mRNA levels
Manually annotated by BRENDA team
-
significantly reduced LPL activity in parametrial adipose tissue from mice fed with conjugated linoleic acid
Manually annotated by BRENDA team
-
decrease of enzyme activity in mesenteric and epididymal white adipose tissue upon chronic stress, accompanied by weight reduction of tissue. Decrease of enzyme activity upon acute stress only in retroperitoneal white adipose tissue
Manually annotated by BRENDA team
-
increase in enzyme activity in presponse to feeding, during 4 h, then decrease to basal levels at 6 h. Fasting produces down-regulation of enzyme activity, concomitant with low levels of plasma insulin. Stimulation of enzyme activity by injection of insulin, especially stimulation of the proportion of enzyme in active conformation at the extracellular level
Manually annotated by BRENDA team
-
range of enzyme activity differs up to 4fold among mink, mice, chinese hamster, rat and guinea pig
Manually annotated by BRENDA team
-
fasting for 2 weeks provokes a clear decrease in activity. Insulin administration induces an increase in activity 3 h after the injection
Manually annotated by BRENDA team
-
limb muscle, increase of enzyme activity and mRNA level upon chronic stress
Manually annotated by BRENDA team
-
aortic endothelial cells
Manually annotated by BRENDA team
-
highest expression is found in aorta
Manually annotated by BRENDA team
-
decreased to 78% and 73% of baseline values 2 h and 4 h after glucose administration, respectively
Manually annotated by BRENDA team
Q06000
postheparin lipoprotein lipase increases by about 200%
Manually annotated by BRENDA team
-
limb muscle, increase of enzyme activity and mRNA level upon chronic and acute stress
Manually annotated by BRENDA team
-
in vivo administration of adrenaline and acute stress causes an increase in plasma lipoprotein lipase activity
Manually annotated by BRENDA team
-
measurable LPL activity is present only in postheparin plasma
Manually annotated by BRENDA team
-
heparin releases LPL from its in vivo binding sites allowing it to enter the blood plasma
Manually annotated by BRENDA team
-
GPIHBP1 shuttles lipoprotein lipase from subendothelial spaces to the capillary lumen
Manually annotated by BRENDA team
-
LPL activity increases in homone-sensitive lipase ko-mice
Manually annotated by BRENDA team
-
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
-
aortic endothelial cells
Manually annotated by BRENDA team
-
tubular epithelial cell
Manually annotated by BRENDA team
-
limb muscle, increase of enzyme activity and mRNA level upon chronic stress
Manually annotated by BRENDA team
-
range of enzyme activity differs up to 6fold among mink, mice, chinese hamster, rat and guinea pig
Manually annotated by BRENDA team
Q06000
when actinomycin is given to fed rats, heparin-releasable lipoprotein lipase activity increases by 160% in 6 h
Manually annotated by BRENDA team
-
activity decreases by 50% on food deprivation for 6 h without corresponding changes in enzyme mRNA or mass. Range of enzyme activity differs up to 500fold among mink, mice, chinese hamster, rat and guinea pig. Mink shows the highest kidney enzyme activity, guinea pig the lowest.
Manually annotated by BRENDA team
-
range of enzyme activity differs up to 500fold among mink, mice, chinese hamster, rat and guinea pig. Mink shows the highest kidney enzyme activity, guinea pig the lowest
Manually annotated by BRENDA team
-
injection of labelled enzyme. Uptake of enzyme through sinusoidal membrane, where it becomes internalized and degraded. Injection of heparin prior to injection of enzyme results in increased enzyme-immunostaining in Kupffer cells. Injection of inactive enzyme also results in increased staining of Kupffer cells
Manually annotated by BRENDA team
-
patient with severe hypertriglyceridemia, post-heparin enzyme mass is almost normal, but the enzyme activity is remarkably decreased
Manually annotated by BRENDA team
-
presence of substantial amounts of inactive enzyme. After injection of heparin, enzyme mass in liver increases, and enzyme activity also increases, but in protportion to mass
Manually annotated by BRENDA team
-
LpL is present in the liver during fetal and early postnatal life, but is then suppressed by a putative transcriptional regulatory mechanism
Manually annotated by BRENDA team
Q6P2U2
highly expressed in liver
Manually annotated by BRENDA team
-
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
-
highest expression is found in lung
Manually annotated by BRENDA team
-
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
-
in the mammary gland, synthesis of LpL is induced during late pregnancy and lactation
Manually annotated by BRENDA team
-
skeletal muscle, cardiac muscle
Manually annotated by BRENDA team
-
limb muscle, increase of enzyme activity and mRNA level upon chronic stress
Manually annotated by BRENDA team
-
red or white muscle, no stimulation of enzyme activity after injection of insulin
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
A4F5E8
LPL is highly expressed and active in the ovary during gonadal development, the LPL mRNA expression is localised to the follicle cells surrounding the oocyte
Manually annotated by BRENDA team
-
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
-
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
-
postheparin
Manually annotated by BRENDA team
Mus musculus ICR
-
-
-
Manually annotated by BRENDA team
-
LPL activity increases in homone-sensitive lipase ko-mice
Manually annotated by BRENDA team
Q06000
soleus, when actinomycin is given to fed rats, heparin-releasable lipoprotein lipase activity increases by 150% in 6 h
Manually annotated by BRENDA team
-
fasting for 2 weeks or insulin administration has no effect on activity
Manually annotated by BRENDA team
-
highest expression in normal testis
Manually annotated by BRENDA team
-
LPL activity increases in homone-sensitive lipase ko-mice
Manually annotated by BRENDA team
-
retroperitoneal white adipose tissue lipoprotein lipase activity is rapidly down-regulated in response to acute stress
Manually annotated by BRENDA team
-
highest expression is found in white adipose tissue
Manually annotated by BRENDA team
additional information
-
LpL mRNA is not detected in peritoneal macrophages or plasma white cells of transgenic mice
Manually annotated by BRENDA team
additional information
A4F5E8
no mRNA transcripts are found in intestine, liver, brain, heart, kidney, muscle, and spleen
Manually annotated by BRENDA team
additional information
-
LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes
Manually annotated by BRENDA team
additional information
Q6P2U2
almost no expression in brain, heart, intestine, and testis
Manually annotated by BRENDA team
additional information
Mus musculus C57BL/6J
-
LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Mus musculus C57BL/6J
-
bound
-
Manually annotated by BRENDA team
-
small pool is present in low density membrane vesicles
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62000
-
gel filtration
80907
64000
-
gel filtratiion
80918
67000
-
gel filtration
80840
75000
-
gel filtration
80901
96900
-
calculation from sedimentation and diffusion data
80887
96900
-
-
80904
100000 - 110000
-
gel filtration
80898
121000
-
gel filtration
80921
123000
-
gel filtration
80921
additional information
-
-
80892
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 56000, SDS-PAGE
?
-
x * 56000, SDS-PAGE
?
-
x * 56000, SDS-PAGE
?
-
x * 58000, SDS-PAGE
?
-
x * 63000, SDS-PAGE
?
-
x * 11000 + x * 16000, ratio 1:1, SDS-PAGE
?
-
x * 34000, SDS-PAGE, equilibrium sedimentation in presence of 6 M guanidine HCl and 0.1% mercaptoethanol
?
-
x * 41700, SDS-PAGE
?
-
x * 60500, SDS-PAGE
?
-
x * 50314, calculation from nucleotide sequence
?
-
x * 60900, SDS-PAGE
dimer
-
-
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 48300, equilibrium sedimentation in guanidine under reducing und nonreducing conditions
dimer
-
2 * 55000, dissociation of the dimer into monomers leads to irreversible loss of activity
dimer
-
inactive in the monomeric state
dimer
-
mass spectrometry, dynamic light scattering. Enzyme is a dynamice dimer in which the subunits rapidly exchange partners. Presence of heparin or lipoproteins does not markedly slow the exchange rate
dimer
-
active enzyme
dimer
Mus musculus C57BL/6J
-
-
-
homodimer
-
-
homodimer
-
dissociation of the dimeric form to the monomeric form is associated with a conformational change of the molecule and irreversible loss of catalytic activity
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 67000, SDS-PAGE
additional information
-
-
additional information
-
heparin-resistant binding of monomeric enzyme to monocytes and macrophages
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
-
side-chain modification
-
glycoprotein
side-chain modification
-
8.3% carbohydrate including mannose, galactose, glucose, N-acetylglucosamine and sialic acid
side-chain modification
-
contains aminosugars
side-chain modification
-
8.3% carbohydrate
side-chain modification
-
-
side-chain modification
-
contains glucosamine
glycoprotein
-
-
glycoprotein
-
2 N-linked glykosylation sites per subunit
side-chain modification
-
glycoprotein
side-chain modification
-
N-glycosylation sites are Asn43 and Asn359
side-chain modification
-
8% carbohydrate, 2% mannose, 2% galactose, 3% glucosamine
glycoprotein
-
-
side-chain modification
-
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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
80895
25
-
no loss of activity after 30 min
651409
25
Q9W6Y2
approx. 20% loss of activity after 30 min
651409
37
-
30% loss of activity after 30 min
651409
37
Q9W6Y2
77% loss of activity after 6 min
651409
37
-
10 min, absence of apop C-II, 15% loss of activity
80888
37
-
rapid loss of activity
80908
40
-
20 min, 50% loss of activity
80894
50
-
pH 5-7, 15 min, stable up to
80900
additional information
-
high concentrations of glycerol or glycine prevent inactivation at 37C and at 4C
80904
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
-
high concentrations of NaCl increase the rate of inactivation
-
heparin has a limited role in stabilizing the bound LPL active dimers
-
the partially purified enzyme at later stages is stabilized by the inclusion of 20% glycerol in the buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 1% serum albumin, 1 h, 60% loss of activity
-
4C, moderate stability
-
-70C, 8 weeks, 20% loss of activity
-
-70C, 1 mg bovine serum albumin per ml or 50% glycerol, stable for several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
biotinylated enzyme by sucrose density gradient centrifugation and heparin affinity chromatography
-
heparin affinity chromatography
-
partial
-
recombinant LPL
-
partial
-
partially purified by heparin-Sepharose column chromatography
-
partially purified using heparin-Sepharose affinity column chromatography
-
recombinant enzyme is purified by TALON metal affinity resin chromatography
-
heparin-Sepharose, partially purified
Q9W6Y2
sedimentation in 10 mM sodium sulfite followed by centrifugation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in HHO cells
-
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
-
expressed in HEK-293 cells
-
expressed in J-774 cells
-
expressed in Mus musculus
-
expressed in Mus musculus mammary glands (milk)
-
expression in COS cells
-
expression in HEK 293 cells
-
expression in rabbit inhibits diet-induced hypercholesterolemia and atherosclerosis
-
expression in Sf21 insect cells, coexpression with calreticulin enhances yield of active LPL by a factor 9
-
expression of LPL mini gene in mice
-
fusion protein consisting of the complete lipoprotein lipase molecule and the mature form of apolipoprotein CII, expression in human embryonic kidney 293 cells
-
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
-
expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during embryogenesis, the mRNA level is increased gradually
Q6P2U2
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
-
stress and catecholamines reduce adipose enzyme activity. Tissue necrosis factpor alpha represses enzyme activity by downregulating transcription
-
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
-
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
-
insulin, dexamethasone and cortisol increase mRNA and activity in adipose organs. Cold markedly stimulates enzyme activity in brown adipose tissue
-
lipoprotein lipase activity is significantly decreased in the ischemic side cortex at 2 h ischemia
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
N291S
-
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease
S447X
-
the mutation is associated with a higher risk for pancreatic calcification and steatorrhea in hyperlipidemic pancreatitis
K430A/R432A/K434A/K440A/K441A
-
the mutant LPL has little or no ability to bind to GPIHBP1 on the surface of cells
additional information
-
chimeric molecule between human lipoprotein lipase and rat hepatic lipase
additional information
-
nonsense mutation Gln106Stop, missense mutations: Gly142Glu, Ala176Thr, Gly188Glu, Ile194Thr, Pro207Leu and Arg243His
additional information
-
chimeric lipase constructed of the N-terminal 329 residues of rat hepatic lipase linked to the C-terminal 136 residues of human lipoprotein lipase. The chimera hydrolyzes both monodisperse short-chain (esterase) and emulsified long-chain (lipase) triacylglycerol substrates with catalytic and kinetic properties closely resembling those of native lipase
additional information
-
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. The chimeric enzyme hydrolyzes both long chain and short chain fatty acid triacylglycerols and has catalytic properties that are similar to lipoprotein lipase
additional information
-
exchanging lids between lipoprotein lipase and endothelial lipase only partially shifts the substrate specificity of the enzymes. Studies of a double chimera possessing both the lid and the C-terminal domain (C-domain) of endothelial lipase in the lipoprotein lipase backbone showed that the role of the lid in determining substrate specificity does not depend on the nature of the C-domain of the lipase
additional information
-
two LPL intronic variants may be associated with development of the hypertension endophenotype with elevated plasma triglycerid level (cSNPs g.7663364C4A in exon 8 and g.7664652C4G in exon 9)
S447X
-
the mutation results in truncation of the last two amino acids of the mature LPL and is the only mutation reported to increase enzymatic activity, the mutation is associated with differential susceptibility to cardiovascular disease
additional information
-
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
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
LITERATURE
medicine
-
heparin-resistant binding of monomeric enzyme to monocytes and macrophages. Enzyme-mediated binding of low density lipoproteins to cell surfaces is enhanced in presence of dexamethasone
medicine
-
comparison of protein and mRNA levels of enzyme and several muscle lipid-binding proteins in healthy, nonobese, nontrained, moderately trained, and endurance-trained women and men. In the nontrained state, women have higher muscle RNA levels of several proteins related to lipid metabolism compared with men. In the endurance-trained state, only the gender difference in lipoprotein lipase mRNA persists
medicine
-
determination of enzyme and of hepatic triacylglycerol lipase activity and comparison with serum adiponectin levels in Japanese hyperlipidemic men. Co-linearity between insulin sensitivity and adiponectin as well as insulin sensitivity and enzyme/hepatic triacylglycerol lipase activity
medicine
-
enzyme significantly suppresses TNF-alpha-induced gene expression, and this suppression is reversed by tetrahydrolipstatin and heparinase. In contrast, enzyme synergistically enhances IFN-gamma-induced gene expression
medicine
-
expression of enzyme in transgenic rabbit, no significant difference in plasma glucose clearance rate between transgenic and control animals. Transgenic animals show reduced plasma levels for free fatty acids and glucose and increased postheparin plasma enzyme activity
medicine
-
measurement of enzyme activity using intravenous fat tolerance test before and after oral administration of glucose. Enzyme activity decreases to 78% and 73% of control levels 2 and 4 h after glucose administration, resp. Use of intravenous fat tolerance test for studying acute changes in enzyme activity
medicine
-
the intravenous fat tolerance test is a promising approach for studying acute changes in LPL activity in circulation
medicine
-
excess vascular wall LpL augments vascular dysfunction in the setting of inflammation
medicine
-
LPL mutations represent a risk factor which contributes to the development of cardiovascular disease
medicine
-
retinoid X receptor gamma-deficient mice, increase in activity of skeletal muscle enzyme isoform, but no increase in enzyme activity in adipose and cardiac tissue. Resistance of animals to gain in fat mass in response to high-fat feeding through up-regulation of enzyme activity in skeletal muscle