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Information on EC 3.1.1.34 - lipoprotein lipase and Organism(s) Bos taurus and UniProt Accession P11151
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3.1.1.34 lipoprotein lipaseIUBMB Comments
Hydrolyses triacylglycerols and diacylglycerol in chylomicrons and low-density lipoprotein particles. Human protein purified from post-heparin plasma (LPL) shows no activity against triglyceride in the absence of added lipoprotein. The principal reaction sequence of that enzyme is triglyceride -> 1,2-diglyceride -> 2-monoglyceride. The hepatic enzyme (LIPC) also hydrolyses triglycerides and phospholipids present in circulating plasma lipoproteins.
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Word Map
- 3.1.1.34
- triglyceride
- cholesterol
-
apolipoproteins
- hdl
- adipocytes
- hypertriglyceridemia
-
lipolysis
-
high-density
-
low-density
- peroxisome
- obesity
- atherosclerosis
- triacylglycerols
- chylomicron
- cardiovascular
-
proliferator-activated
-
post-heparin
- coronary
- milk
-
triglyceride-rich
-
obese
-
remnant
-
postprandial
-
atherogenic
-
high-fat
- hyperlipidemia
- dyslipidemia
-
ppars
- lipases
-
very-low-density
- hyperlipoproteinemia
- preadipocytes
-
lipogenesis
-
depot
-
angiopoietin-like
- epididymal
- leptin
-
normolipidemic
-
adipogenic
-
hormone-sensitive
-
hdl-cholesterol
-
heparin-sepharose
- nefas
-
lecithin:cholesterol
- triolein
- medicine
- intralipid
- synthesis
-
perirenal
- pvuii
-
lipoprotein-cholesterol
- emulsions
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lipoprotein lipase, adipose tissue lpl, dag lipase, diglyceride lipase, clearing factor, postheparin lipase, postheparin esterase, placental lipoprotein lipase, diacylglycerol hydrolase, triacylglycero-protein acylhydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
clearing factor
-
-
-
-
diacylglycerol hydrolase
-
-
-
-
diacylglycerol lipase
-
-
-
-
diglyceride lipase
-
-
-
-
lipemia-clearing factor
-
-
-
-
LPL
postheparin esterase
-
-
-
-
postheparin lipase
-
-
-
-
LPL
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
triacylglycero-protein acylhydrolase
Hydrolyses triacylglycerols and diacylglycerol in chylomicrons and low-density lipoprotein particles. Human protein purified from post-heparin plasma (LPL) shows no activity against triglyceride in the absence of added lipoprotein. The principal reaction sequence of that enzyme is triglyceride -> 1,2-diglyceride -> 2-monoglyceride. The hepatic enzyme (LIPC) also hydrolyses triglycerides and phospholipids present in circulating plasma lipoproteins.
CAS REGISTRY NUMBER
COMMENTARY
9004-02-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-O-dilauryl-DL-glycero-3-glutaric acid-(6-methylresorufin ester) + H2O
?
-
-
-
-
?
1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine + H2O
myristic acid + 2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine
-
-
-
?
EnzChek lipase substrate + H2O
?
-
a commercially available BODIPY, Dabcyl-labeled triglyceride analog substrate, C58H85BF2N6O6
-
-
?
additional information
?
-
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
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
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
-
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
-
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
-
dodecanesulfonyl fluoride
-
0.01 mM-0.02 mM, 50% inhibition, complete inhibition after 24 h
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
Lys-Gly-Glu-Glu
-
not only inhibits the basal activity of lipoprotein lipase, but also blocks the activation effect of native apolipoprotein C II
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
-
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
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 CII
-
100% and 300% of increase in LPL activity for phosphatidyl-choline and triglyceride hydrolysis, respectively
-
apoprotein CII
-
activation of triolein and phosphatidylcholine hydrolysis in emulsions
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of p-nitrophenyl butyrate
0.00028
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of tripropionin
0.00038
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of tributyrin
0.0017
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of tricaprylin
0.0031
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of triacetin
0.0047
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of triolein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
-
-
80883, 80884, 80885, 80887, 80888, 80890, 80904, 80905, 80908, 80913, 80922, 650396, 650554, 652039, 652457, 652703, 665589, 693431, 715654
additional information
-
LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LIPL_BOVIN
478
0
53378
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48300
-
2 * 48300, equilibrium sedimentation in guanidine under reducing und nonreducing conditions
96900
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
heparin-resistant binding of monomeric enzyme to monocytes and macrophages
dimer
-
2 * 48300, equilibrium sedimentation in guanidine under reducing und nonreducing conditions
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
8.3% carbohydrate including mannose, galactose, glucose, N-acetylglucosamine and sialic acid
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W390A
-
decreased activity with monoclonal antibody 5D2, decreased activity against a synthetic emulsion of long-chain triacylglycerols and in particular against rat lymph chylomicrons
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
additional information
-
high concentrations of glycerol or glycine prevent inactivation at 37°C and at 4°C
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
biotinylated enzyme by sucrose density gradient centrifugation and heparin affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lambert, D.A.; Smith, L.C.; Pownall, H.; Sparrow, J.T.; Nicolas, J.P.; Gotto, A.M.
Hydrolysis of phospholipids by purified milk lipoprotein lipase. Effect of apoprotein CII, CIII, A and E, and synthetic fragments
Clin. Chim. Acta
291
19-33
2000
Bos taurus
Connelly, P.W.; Maguire, G.F.; Vezina, C.; Hegele, R.A.; Kuksis, A.
Kinetics of lipolysis of very low density lipoproteins by lipoprotein lipase. Importance of particle number and noncompetitive inhibition by particles with low triglyceride content
J. Biol. Chem.
269
20554-20560
1994
Bos taurus
Lookene, A.; Groot, N.B.; Kastelein, J.J.P.; Olivecrona, G.; Bruin, T.
Mutation of tryptophan residues in lipoprotein lipase. Effects on stability, immunoreactivity, and catalytic properties
J. Biol. Chem.
272
766-772
1997
Bos taurus
Iverius, P.H.; stlund-Lindqvist, A.M.
Preparation, characterization, and measurement of lipoprotein lipase
Methods Enzymol.
129
691-704
1986
Bos taurus, Homo sapiens, Rattus norvegicus
Hayashi, R.; Tajima, S.; Yamamoto, A.
Purification and characterization of lipoprotein lipase from human postheparin plasma and its comparison with purified bovine milk lipoprotein lipase
J. Biochem.
100
319-331
1986
Bos taurus, Homo sapiens
Bengtsson-Olivecrona, G.; Olivecrona, T.; Jrnvall, H.
Lipoprotein lipases from cow, guinea-pig and man. Structural characterization and identification of protease-sensitive internal regions
Eur. J. Biochem.
161
281-288
1986
Bos taurus, Cavia porcellus, Homo sapiens
Olivecrona, T.; Bengtsson, G.; Osborne, J.C.
Molecular properties of lipoprotein lipase. Effects of limited trypsin digestion on molecular weight and secondary structure
Eur. J. Biochem.
124
629-633
1982
Bos taurus
Iverius, P.H.; stlund-Lindqvist, A.M.
Lipoprotein lipase from bovine milk. Isolation procedure, chemical characterization, and molecular weight analysis
J. Biol. Chem.
251
7791-7795
1976
Bos taurus
Kinnunen, P.K.J.; Huttunen, J.K.; Ehnholm, C.
Properties of purified bovine milk lipoprotein lipase
Biochim. Biophys. Acta
450
342-351
1976
Bos taurus
Egelrud, T.; Olivecrona, T.
The purification of a lipoprotein lipase from bovine skim milk
J. Biol. Chem.
247
6212-6217
1972
Bos taurus
Wang, C.S.; Hartsuck, J.; McConathy, J.
Structure and functional properties of lipoprotein lipase
Biochim. Biophys. Acta
1123
1-17
1992
Bos taurus, Cavia porcellus, Gallus gallus, Homo sapiens, Mus musculus
Goldberg, I.J.; Blaner, W.S.; Goodman, D.S.
Immunologic and enzymatic comparisons between human and bovine lipoprotein lipase
Arch. Biochem. Biophys.
244
580-584
1986
Bos taurus, Homo sapiens
LaDu, M.J.; Schultz, C.J.; Essig, D.A.; Palmer, W.K.
Characterization of serum-stimulated lipoprotein lipase from bovine heart
Int. J. Biochem.
23
405-411
1991
Bos taurus
Cheng, Q.; Blackett, P.; Jackson, K.W.; McConathy, W.J.; Wang, C.S.
C-terminal domain of apolipoprotein CII as both activator and competitive inhibitor of lipoprotein lipase
Biochem. J.
269
403-407
1990
Bos taurus
Yamamoto, M.; Morita, S.Y.; Kumon, M.; Kawabe, M.; Nishitsuji, K.; Saito, H.; Vertut-Doi, A.; Nakano, M.; Handa, T.
Effects of plasma apolipoproteins on lipoprotein lipase-mediated lipolysis of small and large lipid emulsions
Biochim. Biophys. Acta
1632
31-39
2003
Bos taurus
Kokotos, G.; Kotsovolou, S.; Constantinou-Kokotou, V.; Wu, G.; Olivecrona, G.
Inhibition of lipoprotein lipase by alkanesulfonyl fluorides
Bioorg. Med. Chem. Lett.
10
2803-2806
2000
Bos taurus
Lindberg, A.; Olivecrona, G.
Lipoprotein lipase from rainbow trout differs in several respects from the enzyme in mammals
Gene
292
213-223
2002
Bos taurus, Homo sapiens, Oncorhynchus mykiss (Q9W6Y2), Oncorhynchus mykiss
Hussain, M.M.; Obunike, J.C.; Shaheen, A.; Hussain, M.J.; Shelness, G.S.; Goldberg, I.J.
High affinity binding between lipoprotein lipase and lipoproteins involves multiple ionic and hydrophobic interactions, does not require enzyme activity, and is modulated by glycosaminoglycans
J. Biol. Chem.
275
29324-29330
2000
Bos taurus
McIlhargey, T.L.; Yang, Y.; Wong, H.; Hill, J.S.
Identification of a lipoprotein lipase cofactor-binding site by chemical cross-linking and transfer of apolipoprotein C-II-responsive lipolysis from lipoprotein lipase to hepatic lipase
J. Biol. Chem.
278
23027-23035
2003
Bos taurus
Lookene, A.; Zhang, L.; Tougu, V.; Olivecrona, G.
1,1'-bis(anilino)-4-,4'-bis(naphtalene)-8,8'-disulfonate acts as an inhibitor of lipoprotein lipase and competes for binding with apolipoprotein CII
J. Biol. Chem.
278
37183-37194
2003
Bos taurus
Rinninger, F.; Brundert, M.; Brosch, I.; Donarski, N.; Budzinski, R.M.; Greten, H.
Lipoprotein lipase mediates an increase in selective uptake of HDL-associated cholesteryl esters by cells in culture independent of scavenger receptor BI
J. Lipid Res.
42
1740-1751
2001
Bos taurus
Makoveichuk, E.; Castel, S.; Vilaro, S.; Olivecrona, G.
Lipoprotein lipase-dependent binding and uptake of low density lipoproteins by THP-1 monocytes and macrophages: possible involvement of lipid rafts
Biochim. Biophys. Acta
1686
37-49
2004
Bos taurus
Neuger, L.; Vilaro, S.; Lopez-Iglesias, C.; Gupta, J.; Olivecrona, T.; Olivecrona, G.
Effects of heparin on the uptake of lipoprotein lipase in rat liver
BMC Physiol.
4
13
2004
Bos taurus, Rattus norvegicus
Lookene, A.; Zhang, L.; Hultin, M.; Olivecrona, G.
Rapid subunit exchange in dimeric lipoprotein lipase and properties of the inactive monomer
J. Biol. Chem.
279
49964-49972
2004
Bos taurus
Zhang, L.; Lookene, A.; Wu, G.; Olivecrona, G.
Calcium triggers folding of lipoprotein lipase into active dimers
J. Biol. Chem.
280
42580-42591
2005
Bos taurus
Andreo, U.; Maillard, P.; Kalinina, O.; Walic, M.; Meurs, E.; Martinot, M.; Marcellin, P.; Budkowska, A.
Lipoprotein lipase mediates hepatitis C virus (HCV) cell entry and inhibits HCV infection
Cell. Microbiol.
9
2445-2456
2007
Homo sapiens, Bos taurus (P11151)
Pak-Dek, M.S.; Abdul-Hamid, A.; Osman, A.; Soh, C.S.
Inhibitory effect of Morinda citrifolia L. on lipoprotein lipase activity
J. Food Sci.
73
C595-C598
2008
Bos taurus
Yau, M.H.; Wang, Y.; Lam, K.S.; Zhang, J.; Wu, D.; Xu, A.
A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization
J. Biol. Chem.
284
11942-11952
2009
Bos taurus, Mus musculus, Mus musculus C57/BL6J
Nishitsuji, K.; Hosono, T.; Uchimura, K.; Michikawa, M.
Lipoprotein lipase is a novel amyloid beta (Abeta)-binding protein that promotes glycosaminoglycan-dependent cellular uptake of Abeta in astrocytes
J. Biol. Chem.
286
6393-6401
2011
Bos taurus
Basu, D.; Manjur, J.; Jin, W.
Determination of lipoprotein lipase activity using a novel fluorescent lipase assay
J. Lipid Res.
52
826-832
2011
Bos taurus, Mus musculus
Shimizu, Y.; Hishiki, T.; Sugiyama, K.; Ogawa, K.; Funami, K.; Kato, A.; Ohsaki, Y.; Fujimoto, T.; Takaku, H.; Shimotohno, K.
Lipoprotein lipase and hepatic triglyceride lipase reduce the infectivity of hepatitis C virus (HCV) through their catalytic activities on HCV-associated lipoproteins
Virology
407
152-159
2010
Bos taurus
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