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Information on EC 3.1.1.34 - lipoprotein lipase and Organism(s) Rattus norvegicus and UniProt Accession Q06000

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.34 lipoprotein lipase
IUBMB 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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This record set is specific for:
Rattus norvegicus
UNIPROT: Q06000
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
clearing factor
-
-
-
-
DAG lipase
-
-
diacylglycerol hydrolase
-
-
-
-
diacylglycerol lipase
diglyceride lipase
-
-
-
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lipemia-clearing factor
-
-
-
-
postheparin esterase
-
-
-
-
postheparin lipase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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 hide
9004-02-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chylomicron + H2O
?
show the reaction diagram
-
-
-
-
?
chylomicrons + H2O
?
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
trioctanoin + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleate + diolein
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
-
-
-
-
?
very-low-density lipoproteins + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antiserum to rat adipose tissue lipoprotein lipase
-
-
-
apolipoprotein C I
-
-
-
apolipoprotein C III
-
-
-
cytochalasin D
-
preincubation with cytochalasin D prevents the increase in dexmethasone-induced lipoprotein lipase activity
diisopropyl fluorophosphate
-
-
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
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
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0.5 M, 80% inhibition, 1 M, 90% inhibition
phenylmethylsulfonyl fluoride
-
-
Protamine sulfate
-
-
-
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
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81.8% relative activity in the presence of 5% (w/v) sodium deoxycholate
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
apolipoprotein C-II
-
dexamethasone
-
induces increase in coronary lipoprotein lipase, combination of 100 nM dexmethasone with 100 nM insulin appreciably enhances lipoprotein lipase activity
Gum arabic
-
197.6% relative activity in the presence of 1% (w/v) Gum Arabic, emulsifier for determination of LPL activity
-
heparin
Insulin
-
combination of 100 nM dexmethasone with 100 nM insulin appreciably enhances lipoprotein lipase activity
-
serum
-
stimulates
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Tween 80
-
409.6% relative activity in the presence of 5% (v/v) Tween 80
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.77
chylomicron
-
-
-
0.075 - 0.083
chylomicrons
-
soluble enzyme
-
1.57
triolein
-
-
1.62 - 1.68
very-low-density lipoprotein
-
0.026 - 0.053
Very-low-density lipoproteins
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
precursor
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
postheparin lipoprotein lipase increases by about 200%
Manually annotated by BRENDA team
when actinomycin is given to fed rats, heparin-releasable lipoprotein lipase activity increases by 160% in 6 h
Manually annotated by BRENDA team
soleus, when actinomycin is given to fed rats, heparin-releasable lipoprotein lipase activity increases by 150% in 6 h
Manually annotated by BRENDA team
-
limb muscle, increase of enzyme activity and mRNA level upon chronic stress
Manually annotated by BRENDA team
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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
-
SCG neurons
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
small pool is present in low density membrane vesicles
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIPL_RAT
474
0
53082
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
-
x * 11000 + x * 16000, ratio 1:1, SDS-PAGE
123000
-
gel filtration
16000
-
x * 11000 + x * 16000, ratio 1:1, SDS-PAGE
34000
-
x * 34000, SDS-PAGE, equilibrium sedimentation in presence of 6 M guanidine HCl and 0.1% mercaptoethanol
56000
-
x * 56000, SDS-PAGE
60000
-
2 * 60000, SDS-PAGE
75000
-
gel filtration
additional information
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
-
-
additional information
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
side-chain modification
-
glycoprotein
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 8 weeks, 20% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sedimentation in 10 mM sodium sulfite followed by centrifugation
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
lipoprotein lipase activity is significantly decreased in the ischemic side cortex at 2 h ischemia
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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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Vydelingum, N.A.; AlQuadan, F.; Kissebah, A.H.; Etienne, J.
Characterization of rat adipose tissue lipoprotein lipase using a monospecific antibody
Biochim. Biophys. Acta
876
399-412
1986
Rattus norvegicus
Manually annotated by BRENDA team
Al-Jafari, A.A.; Chyer, A.
The lipoprotein lipase of white adipose tissue. Studies on the intracellular distribution of the adipocyte-associated enzyme
Biochem. J.
236
749-756
1986
Cavia porcellus, Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Friedman, G.; Chajek-Shaul, T.; Etienne, J.; Stein, O.; Stein, Y.
Characterization of the lipoprotein lipase in the functional pool of rat heart by immunoblotting
Biochim. Biophys. Acta
875
379-399
1986
Rattus norvegicus
-
Manually annotated by BRENDA team
Parkin, S.M.; Speake, B.K.; Robinson, D.S.
Purification and characterization of rat adipose tissue lipoprotein lipase
Biochem. J.
207
485-495
1982
Rattus norvegicus
Manually annotated by BRENDA team
Clegg, R.A.
Lipoprotein lipase in lactating rat mammary tissue: purification, characterization and surface location on isolated mammary cells [proceedings
Biochem. Soc. Trans.
7
1053-1054
1979
Rattus norvegicus
Manually annotated by BRENDA team
Chung, J.; Scanu, A.M.
Isolation, molecular properties, and kinetic characterization of lipoprotein lipase from rat heart
J. Biol. Chem.
252
4202-4209
1977
Rattus norvegicus
Manually annotated by BRENDA team
Fielding, C.J.; Higgins, J.M.
Lipoprotein lipase: comparative properties of the membrane-supported and solubilized enzyme species
Biochemistry
13
4324-4330
1974
Rattus norvegicus
Manually annotated by BRENDA team
Sato, K.; Suzuki, K.; Akiba, Y.
Species differences in substrate specificity of lipoprotein lipase purified from chicken and rats
Comp. Biochem. Physiol. A
119
569-573
1998
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Rogers, M.P.; Dale, A.; Etienne, J.; Younan, S.
Lipoprotein lipase in heart and myocytes: characteristics with intralipid as substrate
Comp. Biochem. Physiol. B
101
327-331
1992
Rattus norvegicus
Manually annotated by BRENDA team
Soteriou, A.; Cryer, A.
Purification and characterization of lipoprotein lipase from the white adipose, skeletal muscle, cardiac muscle, mammary gland and lung tissues of the rat
Int. J. Biochem.
25
1483-1490
1993
Rattus norvegicus
Manually annotated by BRENDA team
Sato, K.; Akiba, Y.; Horiguchi, M.
Species differences between chickens and rats in chemical properties of adipopse tissue lipoprotein lipase
Comp. Biochem. Physiol. A
118
855-858
1997
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Ranganathan, G.; Li, C.; Kern, P.A.
The translational regulation of lipoprotein lipase in diabetic rats involves the 3'-untranslated region of the lipoprotein lipase mRNA
J. Biol. Chem.
275
40986-40991
2000
Rattus norvegicus
Manually annotated by BRENDA team
Roh, C.; Roduit, R.; Thorens, B.; Fried, S.; Kandror, K.V.
Lipoprotein lipase and leptin are accumulated in different secretory compartments in rat adipocytes
J. Biol. Chem.
276
35990-35994
2001
Rattus norvegicus
Manually annotated by BRENDA team
Davies, P.J.; Berry, S.A.; Shipley, G.L.; Eckel, R.H.; Hennuyer, N.; Crombie, D.L.; Ogilvie, K.M.; Peinado-Onsurbe, J.; Fievet, C.; Leibowitz, M.D.; Heyman, R.A.; Auwerx, J.
Metabolic effects of rexinoids: tissue-specific regulation of lipoprotein lipase activity
Mol. Pharmacol.
59
170-176
2001
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Ruge, T.; Sukonina, V.; Myrnas, T.; Lundgren, M.; Eriksson, J.W.; Olivecrona, G.
Lipoprotein lipase activity/mass ratio is higher in omental than in subcutaneous adipose tissue
Eur. J. Clin. Invest.
36
16-21
2006
Cavia porcellus, Cricetulus griseus, Mus musculus, Rattus norvegicus, Mustela lutreola
Manually annotated by BRENDA team
Ricart-Jane, D.; Cejudo-Martin, P.; Peinado-Onsurbe, J.; Lopez-Tejero, M.D.; Llobera, M.
Changes in lipoprotein lipase modulate tissue energy supply during stress
J. Appl. Physiol.
99
1343-1351
2005
Rattus norvegicus
Manually annotated by BRENDA team
Wu, G.; Zhang, L.; Gupta, J.; Olivecrona, G.; Olivecrona, T.
A transcription-dependent mechanism, akin to that in adipose tissue, modulates lipoprotein lipase activity in rat heart
Am. J. Physiol. Endocrinol. Metab.
293
E908-E915
2007
Rattus norvegicus (Q06000)
Manually annotated by BRENDA team
Casanovas, A.; Parramon, N.; de la Cruz, F.; Andres, O.; Terencio, J.; Lopez-Tejero, M.D.; Llobera, M.
Retroperitoneal white adipose tissue lipoprotein lipase activity is rapidly down-regulated in response to acute stress
J. Lipid Res.
48
863-868
2007
Rattus norvegicus
Manually annotated by BRENDA team
Kewalramani, G.; Puthanveetil, P.; Kim, M.S.; Wang, F.; Lee, V.; Hau, N.; Beheshti, E.; Ng, N.; Abrahani, A.; Rodrigues, B.
Acute dexamethasone-induced increase in cardiac lipoprotein lipase requires activation of both Akt and stress kinases
Am. J. Physiol. Endocrinol. Metab.
295
E137-E147
2008
Rattus norvegicus
Manually annotated by BRENDA team
Chou, Y.C.; Tsai, Y.C.; Chen, C.M.; Chen, S.M.; Lee, J.A.
Determination of lipoprotein lipase activity in post heparin plasma of streptozotocin-induced diabetic rats by high-performance liquid chromatography with fluorescence detection
Biomed. Chromatogr.
22
502-510
2008
Rattus norvegicus
Manually annotated by BRENDA team
Ricart-Jane, D.; Casanovas, A.; Jane, N.; Gonzalez, M.A.; Buira-Morell, I.; Ribera, J.; Llobera, M.; Lopez-Tejero, M.D.
Nitric oxide and the release of lipoprotein lipase from white adipose tissue
Cell. Physiol. Biochem.
22
525-530
2008
Rattus norvegicus
Manually annotated by BRENDA team
Kim, M.S.; Wang, F.; Puthanveetil, P.; Kewalramani, G.; Hosseini-Beheshti, E.; Ng, N.; Wang, Y.; Kumar, U.; Innis, S.; Proud, C.G.; Abrahani, A.; Rodrigues, B.
Protein kinase D is a key regulator of cardiomyocyte lipoprotein lipase secretion after diabetes
Circ. Res.
103
252-260
2008
Rattus norvegicus
Manually annotated by BRENDA team
Boualga, A.; Prost, J.; Taleb-Senouci, D.; Krouf, D.; Kharoubi, O.; Lamri-Senhadji, M.; Belleville, J.; Bouchenak, M.
Purified chickpea or lentil proteins impair VLDL metabolism and lipoprotein lipase activity in epididymal fat, but not in muscle, compared to casein, in growing rats
Eur. J. Nutr.
48
162-169
2009
Rattus norvegicus
Manually annotated by BRENDA team
Shearer, G.C.; Newman, J.W.
Lipoprotein lipase releases esterified oxylipins from very low-density lipoproteins
Prostaglandins Leukot. Essent. Fatty Acids
79
215-222
2008
Rattus norvegicus
Manually annotated by BRENDA team
Liu, L.; Heneghan, J.F.; Michael, G.J.; Stanish, L.F.; Egertova, M.; Rittenhouse, A.R.
L- and N-current but not M-current inhibition by M1 muscarinic receptors requires DAG lipase activity
J. Cell. Physiol.
216
91-100
2008
Rattus norvegicus
Manually annotated by BRENDA team
Wang, X.; Sun, W.; Xu, E.
The expression and activity of brain lipoprotein lipase is increased after acute cerebral ischemia-reperfusion in rats
Neuropathology
30
131-139
2010
Rattus norvegicus
Manually annotated by BRENDA team