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Information on EC 3.1.1.79 - hormone-sensitive lipase and Organism(s) Homo sapiens and UniProt Accession Q05469

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.79 hormone-sensitive lipase
IUBMB Comments
This enzyme is a serine hydrolase. Compared with other lipases, hormone-sensitive lipase has a uniquely broad substrate specificity. It hydrolyses all acylglycerols (triacylglycerol, diacylglycerol and monoacylglycerol) [2,3,4] as well as cholesteryl esters [2,4], steroid fatty acid esters , retinyl esters and p-nitrophenyl esters [4,7]. It exhibits a preference for the 1- or 3-ester bond of its acylglycerol substrate compared with the 2-ester bond . The enzyme shows little preference for the fatty acids in the triacylglycerol, although there is some increase in activity with decreasing chain length. The enzyme activity is increased in response to hormones that elevate intracellular levels of cAMP.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q05469
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
13-HSL, cardiac HSL, cold-active hormone-sensitive lipase, Est25, EstE5, EstE5 protein, hormone-sensitive lipase, HSL, HSL protein, HSL1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hormone-sensitive lipase
HSL protein
247
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
diacylglycerol acylhydrolase
This enzyme is a serine hydrolase. Compared with other lipases, hormone-sensitive lipase has a uniquely broad substrate specificity. It hydrolyses all acylglycerols (triacylglycerol, diacylglycerol and monoacylglycerol) [2,3,4] as well as cholesteryl esters [2,4], steroid fatty acid esters [5], retinyl esters [6] and p-nitrophenyl esters [4,7]. It exhibits a preference for the 1- or 3-ester bond of its acylglycerol substrate compared with the 2-ester bond [8]. The enzyme shows little preference for the fatty acids in the triacylglycerol, although there is some increase in activity with decreasing chain length. The enzyme activity is increased in response to hormones that elevate intracellular levels of cAMP.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-62-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dioleoyl-sn-glycerol + H2O
?
show the reaction diagram
-
-
-
-
?
cholesteryl oleate + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
trioleoylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
1,2-dioleoyl-sn-glycerol + H2O
2-oleylglycerol + oleate
show the reaction diagram
-
-
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
show the reaction diagram
-
-
-
-
?
diacylglycerol + H2O
monoacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
dioleoyl glycerol + H2O
monooleoylglycerol + oleate
show the reaction diagram
-
21% of activity with vinylbutyrate
-
-
?
lipid emulsion + H2O
fatty acids
show the reaction diagram
-
recombinant HSL, the release of fatty acids is only slightly affected by their degree of unsaturation
fatty acids ranging in chain length from 12 to 24 carbon atoms and in unsaturation from 0 to 6 double bonds
-
?
olive oil + H2O
?
show the reaction diagram
-
3% of activity with vinylbutyrate
-
-
-
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
rac 1,2(2,3)-sn diolein + H2O
?
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
tributanoyl glycerol + H2O
dibutanoylglycerol + butanoate
show the reaction diagram
-
8% of activity with vinylbutyrate
-
-
?
tributanoylglycerol + H2O
dibutanoylglycerol + butanoate
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
dibutanoylglycerol + butanoate
show the reaction diagram
-
-
-
-
?
trioctanoin + H2O
dioctanoylglycerol + octanoate
show the reaction diagram
-
-
-
-
?
trioctanoyl glycerol + H2O
dioctanoylglycerol + octanoate
show the reaction diagram
-
3% of activity with vinylbutyrate
-
-
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
show the reaction diagram
-
-
-
-
?
tripropionin + H2O
dipropanoylglycerol + propanoate
show the reaction diagram
-
-
-
-
?
tripropionyl glycerol + H2O
dipropionylglycerol + propionate
show the reaction diagram
-
4% of activity with vinylbutyrate
-
-
?
vinyl acetate + H2O
acetate + ethylenol
show the reaction diagram
-
-
-
-
?
vinyl acetate + H2O
vinyl alcohol + acetate
show the reaction diagram
-
67% of activity with vinylbutyrate
-
-
?
vinyl butyrate + H2O
butanoate + ethylenol
show the reaction diagram
-
-
-
-
?
vinyl butyrate + H2O
vinyl alcohol + butanoate
show the reaction diagram
-
-
-
-
?
vinyl laurate + H2O
laurate + ethylenol
show the reaction diagram
-
-
-
-
?
vinyl laurate + H2O
vinyl alcohol + laurate
show the reaction diagram
-
15% of activity with vinylbutyrate
-
-
?
vinyl propionate + H2O
propanoate + ethylenol
show the reaction diagram
-
-
-
-
?
vinyl propionate + H2O
vinyl alcohol + propionate
show the reaction diagram
-
50% of activity with vinylbutyrate
-
-
?
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
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3,4-dihydro-1H-isoquinolin-2-yl)-carbamic acid 4-tert-butoxycarbonylamino-phenyl ester
-
IC50: 3 nM
(S)-4-isopropyl-3-methyl-2-[3-methylpiperidine-1-carbonyl]isoxazol-5[2H]-one
-
-
2-methoxyphenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
-
IC50: 6400 nM
3-(3,5-dichlorophenyl)-N,N-dimethyl-5-(methylsulfanyl)-1H-1,2,4-triazole-1-carboxamide
-
-
3-(3-chloro-5-(trifluoromethyl)pyridin-2-yl)-5-ethoxy-1,3,4-oxadiazol-2(3H)-one
-
-
3-(4-chlorophenyl)-N,N-dimethyl-5-(methylsulfanyl)-1H-1,2,4-triazole-1-carboxamide
-
-
4-(acetylamino)phenyl morpholin-4-ylcarbamate
-
-
4-(butyrylamino)phenyl morpholin-4-ylcarbamate
-
IC50: 3200 nM
4-benzoylphenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
-
-
4-benzylphenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
-
IC50: 97 nM
4-chlorophenyl (1-methyl-3,4-dihydroisoquinolin-2(1H)-yl)carbamate
-
IC50: 32 nM
4-chlorophenyl (3-methyl-3,4-dihydroisoquinolin-2(1H)-yl)carbamate
-
IC50: 35 nM
4-chlorophenyl 2,2-bis(2-ethoxyethyl)hydrazinecarboxylate
-
IC50: 184 nM
4-chlorophenyl 2,2-dipentylhydrazinecarboxylate
-
IC50: 50 nM
4-chlorophenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
-
IC50: 19 nM
4-isopropyl-3-methyl-2-[piperidine-1-carbonyl]isoxazol-5[2H]-one
-
-
4-methoxyphenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
-
IC50: 360 nM
4-[(2,2-dimethylpropanoyl)amino]phenyl morpholin-4-ylcarbamate
-
IC50: 47 nM
4-[(cyclohexylcarbonyl)amino]phenyl morpholin-4-ylcarbamate
-
IC50: 10 nM
benzyl (4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)-2-methylphenyl)carbamate
-
-
benzyl (4-[[(morpholin-4-ylamino)carbonyl]oxy]phenyl)acetate
-
IC50: 5 nM
Diethyl p-nitrophenyl phosphate
-
100fold molar excess, complete inactivation after 15 min
diethyl-p-nitrophenyl phosphate
-
0.1 mM, 94% inhibition
diisopropyl fluorophosphate
ethyl (4-[[(morpholin-4-ylamino)carbonyl]oxy]phenyl)acetate
-
IC50: 138 nM
Hg2+
-
0.1 mM, 91% inhibition
HgCl2
-
0.1 mM, 93% inhibition
methyl 4-[[(3,4-dihydroisoquinolin-2(1H)-ylamino)carbonyl]oxy]benzoate
-
IC50: 9952 nM
morpholin-4-yl-carbamic acid 4-[(4-tert-butyl-cyclohexanecarbonyl)-amino]-phenyl ester
-
IC50: 1 nM
N',N'-bis-(2-butylamino-ethyl)-hydrazinecarboxylic acid 4-chloro-phenyl ester
-
IC50: 24 nM
N',N'-bis-[2-(ethyl-methyl-amino)-ethyl]-hydrazinecarboxylic acid 4-chloro-phenyl ester
-
IC50: 515 nM
phenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
-
IC50: 205 nM
phenylmethylsulfonyl fluoride
-
100fold molar excess, complete inactivation after 15 min
additional information
-
hormone-sensitive lipase is knocked down by RNA interference or selectively inhibited
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
tributanoyl glycerol
-
37°C, pH 8.0
0.4
tributyrin
-
-
15
tripropionin
-
-
15
tripropionyl glycerol
-
37°C, pH 8.0
170 - 315
vinyl acetate
10 - 25
vinyl butyrate
4
vinyl laurate
-
-
70 - 75
vinyl propionate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
190
p-nitrophenyl butyrate
-
-
18
tributyrin
-
-
6
trioctanoin
-
-
7
tripropionin
-
-
170
vinyl acetate
-
-
625
vinyl butyrate
-
-
375
vinyl laurate
-
-
800
vinyl propionate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000003
(3,4-dihydro-1H-isoquinolin-2-yl)-carbamic acid 4-tert-butoxycarbonylamino-phenyl ester
Homo sapiens
-
IC50: 3 nM
0.000005
(S)-4-isopropyl-3-methyl-2-[3-methylpiperidine-1-carbonyl]isoxazol-5[2H]-one
Homo sapiens
-
-
0.0064
2-methoxyphenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
Homo sapiens
-
IC50: 6400 nM
0.000008
3-(4-chlorophenyl)-N,N-dimethyl-5-(methylsulfanyl)-1H-1,2,4-triazole-1-carboxamide
Homo sapiens
-
-
0.0032
4-(butyrylamino)phenyl morpholin-4-ylcarbamate
Homo sapiens
-
IC50: 3200 nM
0.000097
4-benzylphenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
Homo sapiens
-
IC50: 97 nM
0.000032
4-chlorophenyl (1-methyl-3,4-dihydroisoquinolin-2(1H)-yl)carbamate
Homo sapiens
-
IC50: 32 nM
0.000035
4-chlorophenyl (3-methyl-3,4-dihydroisoquinolin-2(1H)-yl)carbamate
Homo sapiens
-
IC50: 35 nM
0.000184
4-chlorophenyl 2,2-bis(2-ethoxyethyl)hydrazinecarboxylate
Homo sapiens
-
IC50: 184 nM
0.00005
4-chlorophenyl 2,2-dipentylhydrazinecarboxylate
Homo sapiens
-
IC50: 50 nM
0.000019
4-chlorophenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
Homo sapiens
-
IC50: 19 nM
0.00036
4-methoxyphenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
Homo sapiens
-
IC50: 360 nM
0.000047
4-[(2,2-dimethylpropanoyl)amino]phenyl morpholin-4-ylcarbamate
Homo sapiens
-
IC50: 47 nM
0.00001
4-[(cyclohexylcarbonyl)amino]phenyl morpholin-4-ylcarbamate
Homo sapiens
-
IC50: 10 nM
0.000005
benzyl (4-[[(morpholin-4-ylamino)carbonyl]oxy]phenyl)acetate
Homo sapiens
-
IC50: 5 nM
0.000138
ethyl (4-[[(morpholin-4-ylamino)carbonyl]oxy]phenyl)acetate
Homo sapiens
-
IC50: 138 nM
0.009952
methyl 4-[[(3,4-dihydroisoquinolin-2(1H)-ylamino)carbonyl]oxy]benzoate
Homo sapiens
-
IC50: 9952 nM
0.000001
morpholin-4-yl-carbamic acid 4-[(4-tert-butyl-cyclohexanecarbonyl)-amino]-phenyl ester
Homo sapiens
-
IC50: 1 nM
0.000024
N',N'-bis-(2-butylamino-ethyl)-hydrazinecarboxylic acid 4-chloro-phenyl ester
Homo sapiens
-
IC50: 24 nM
0.000515
N',N'-bis-[2-(ethyl-methyl-amino)-ethyl]-hydrazinecarboxylic acid 4-chloro-phenyl ester
Homo sapiens
-
IC50: 515 nM
0.000205
phenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
Homo sapiens
-
IC50: 205 nM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00059
women
0.00062
men
1.2
-
specific activity of the purified wild type enzyme against trioleoylglycerol
2.3
-
specific activity of the purified wild type enzyme against cholesteryl oleate
23
-
specific activity of the purified wild type enzyme against 1,2-dioleoyl-sn-glycerol
50
-
specific activity of the purified wild type enzyme against p-nitrophenylbutyrate
143
-
hydrolysis of vinyl butyrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
women with polycystic ovary syndrome or obesity have significantly decreased expression of hormone-sensitive lipase. Knock down of hormone-sensitive lipase by RNAi reduces basal and catecholamine-induced lipolysis. Treatment of mesenchymal stem cells with a selective inhibitor of hormone-sensitive lipase during and/or after differentiation in adipocytes reduces basal lipolysis by 50%
Manually annotated by BRENDA team
-
HEK-293 fibroblasts stably expressing fatty acid transport protein 1
Manually annotated by BRENDA team
-
activity is similar in untrained and trained skeletal muscles both before and after prolonged exercise
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
containing hormone-sensitive lipase. In response to insulin the enzyme is translocated to the cytosol
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme expression is abolished in the slit-skin smear specimens from patients with lepromatous and borderline leprosy caused by Mycobacterium leprae, which suppresses lipid degradation through inhibition of enzyme expression
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
LIPS_HUMAN
1076
0
116598
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84000
Western blot
84000
-
2 * 84000, SDS-PAGE, recombinant HSL
84032
-
x * 84032, deduced from nucleotide sequence
88000
-
x * 88000, SDS-PAGE
88200
-
x * 88200, SDS-PAGE, immunoblot
116000
-
x * 116000, SDS-PAGE, testis HSL
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 84000, SDS-PAGE, recombinant HSL
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S552A/S554A
-
variant AVA-SS, no effect on the activity
S552E/S554E
-
variant AVA-AA, decreasing activity of human HSL against trioleoylglycerol, 1,2-dioleoyl-sn-glycerol and cholesteryl oleate substrates by 67%, 63% and 60%, respectively. The activity against p-nitrophenylbutyrate also decreases, but only by 30% compared to wild type HSL
S554A
-
variant SVA-SS, resulted in a slight decrease in lipolytic activity
S554E
-
variant SVE-SS, resulted in similar to wild type activity
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
anion exchange chromatography followed by nickel affinity chromatography and dialysis
-
partially purified, Q-Sepharose FF
-
recombinant HSL
-
recombinant human HSL from baculovirus-infected insect cells
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
five C-terminally His-tagged human HSL variants are successfully cloned and expressed in Sf9 insect cells using the baculovirus/insect cell expression system
-
cloning of cDNA
-
expression Sf9 insect cells
-
human HSL is expressed from baculovirus-infected insect cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
infection by live Mycobacterium leprae significantly suppresses the enzyme expression levels. This suppression is not observed with dead Mycobacterium leprae or latex bead controls
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
monitoring of enzyme mRNA levels in slit-skin smear specimens from patients with lepromatous and borderline leprosy may be a useful indicator of patient prognosis
medicine
-
inhibition of hormone-sensitive lipase may improve insulin sensitivity and blood glucose handling in type 2 diabetes. The utility of enzyme inhibition in diabetes treatment will depend on the presence or absence of adverse effects of inhibition in tissues beyond the adipocyte
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yeaman, S.J.
Hormone-sensitive lipase - new roles for an old enzyme
Biochem. J.
379
11-22
2004
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Remaury, A.; Laurell, H.; Grober, J.; Reynisdottir, S.; Dauzats, M.; Holm, C.; Langin, D.
Expression of hormone-sensitive lipase in the human colon adenocarcinoma cell line HT29
Biochem. Biophys. Res. Commun.
207
175-182
1995
Homo sapiens
Manually annotated by BRENDA team
Mairal, A.; Melaine, N.; Laurell, H.; Grober, J.; Holst, L.S.; Guillaudeux, T.; Holm, C.; Jegou, B.; Langin, D.
Characterization of a novel testicular form of human hormone-sensitive lipase
Biochem. Biophys. Res. Commun.
291
286-290
2002
Homo sapiens
Manually annotated by BRENDA team
Ben Ali, Y.; Chahinian, H.; Petry, S.; Muller, G.; Carriere, F.; Verger, R.; Abousalham, A.
Might the kinetic behavior of hormone-sensitive lipase reflect the absence of the lid domain?
Biochemistry
43
9298-9306
2004
Homo sapiens
Manually annotated by BRENDA team
Holm, C.; Belfrage, P.; Fredrikson, G.
Human adipose tissue hormone-sensitive lipase: identification and comparison with other species
Biochim. Biophys. Acta
1006
193-197
1989
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Osterlund, T.
Structure-function relationships of hormone-sensitive lipase
Eur. J. Biochem.
268
1899-1907
2001
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Raclot, T.; Holm, C.; Langin, D.
Fatty acid specificity of hormone-sensitive lipase: implication in the selective hydrolysis of triacylglycerols
J. Lipid Res.
42
2049-2057
2001
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L.
Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases
Biochim. Biophys. Acta
1738
29-36
2005
Homo sapiens
Manually annotated by BRENDA team
De Jong, J.C.; Sorensen, L.G.; Tornqvist, H.; Jacobsen, P.
Carbazates as potent inhibitors of hormone-sensitive lipase
Bioorg. Med. Chem. Lett.
14
1741-1744
2004
Homo sapiens
Manually annotated by BRENDA team
O'Neill, M.; Watt, M.J.; Heigenhauser, G.J.; Spriet, L.L.
Effects of reduced free fatty acid availability on hormone-sensitive lipase activity in human skeletal muscle during aerobic exercise
J. Appl. Physiol.
97
1938-1945
2004
Homo sapiens
Manually annotated by BRENDA team
Ben Ali, Y.; Carriere, F.; Verger, R.; Petry, S.; Muller, G.; Abousalham, A.
Continuous monitoring of cholesterol oleate hydrolysis by hormone-sensitive lipase and other cholesterol esterases
J. Lipid Res.
46
994-1000
2005
Homo sapiens
Manually annotated by BRENDA team
Claus, T.H.; Lowe, D.B.; Liang, Y.; Salhanick, A.I.; Lubeski, C.K.; Yang, L.; Lemoine, L.; Zhu, J.; Clairmont, K.B.
Specific inhibition of hormone-sensitive lipase improves lipid profile while reducing plasma glucose
J. Pharmacol. Exp. Ther.
315
1396-1402
2005
Homo sapiens
Manually annotated by BRENDA team
Roepstorff, C.; Vistisen, B.; Donsmark, M.; Nielsen, J.N.; Galbo, H.; Green, K.A.; Hardie, D.G.; Wojtaszewski, J.F.; Richter, E.A.; Kiens, B.
Regulation of hormone-sensitive lipase activity and Ser563 and Ser565 phosphorylation in human skeletal muscle during exercise
J. Physiol.
560
551-562
2004
Homo sapiens
Manually annotated by BRENDA team
Watt, M.J.; Spriet, L.L.
Regulation and role of hormone-sensitive lipase activity in human skeletal muscle
Proc. Nutr. Soc.
63
315-322
2004
Homo sapiens
Manually annotated by BRENDA team
Roepstorff, C.; Donsmark, M.; Thiele, M.; Vistisen, B.; Stewart, G.; Vissing, K.; Schjerling, P.; Hardie, D.G.; Galbo, H.; Kiens, B.
Sex differences in hormone-sensitive lipase expression, activity, and phosphorylation in skeletal muscle at rest and during exercise
Am. J. Physiol. Endocrinol. Metab.
291
E1106-E1114
2006
Homo sapiens
Manually annotated by BRENDA team
Ryden, M.; Jocken, J.; van Harmelen, V.; Dicker, A.; Hoffstedt, J.; Wiren, M.; Blomqvist, L.; Mairal, A.; Langin, D.; Blaak, E.; Arner, P.
Comparative studies of the role of hormone-sensitive lipase and adipose triglyceride lipase in human fat cell lipolysis
Am. J. Physiol. Endocrinol. Metab.
292
E1847-E1855
2007
Homo sapiens, Homo sapiens (Q05469)
Manually annotated by BRENDA team
Aboulaich, N.; Ortegren, U.; Vener, A.V.; Stralfors, P.
Association and insulin regulated translocation of hormone-sensitive lipase with PTRF
Biochem. Biophys. Res. Commun.
350
657-661
2006
Homo sapiens
Manually annotated by BRENDA team
Palin, S.L.; McTernan, P.G.; McGee, K.C.; Sturdee, D.W.; Barnett, A.H.; Kumar, S.
Dydrogesterone and norethisterone regulate expression of lipoprotein lipase and hormone-sensitive lipase in human subcutaneous abdominal adipocytes
Diabetes Obes. Metab.
9
585-590
2007
Homo sapiens
Manually annotated by BRENDA team
Helge, J.W.; Biba, T.O.; Galbo, H.; Gaster, M.; Donsmark, M.
Muscle triacylglycerol and hormone-sensitive lipase activity in untrained and trained human muscles
Eur. J. Appl. Physiol.
97
566-572
2006
Homo sapiens
Manually annotated by BRENDA team
Smith, A.J.; Thompson, B.R.; Sanders, M.A.; Bernlohr, D.A.
Interaction of the adipocyte fatty acid-binding protein with the hormone-sensitive lipase: regulation by fatty acids and phosphorylation
J. Biol. Chem.
282
32424-32432
2007
Homo sapiens
Manually annotated by BRENDA team
Fernandez, C.; Hansson, O.; Nevsten, P.; Holm, C.; Klint, C.
Hormone-sensitive lipase is necessary for normal mobilization of lipids during submaximal exercise
Am. J. Physiol. Endocrinol. Metab.
295
E179-E186
2008
Homo sapiens (Q05469)
Manually annotated by BRENDA team
Jocken, J.W.; Roepstorff, C.; Goossens, G.H.; van der Baan, P.; van Baak, M.; Saris, W.H.; Kiens, B.; Blaak, E.E.
Hormone-sensitive lipase serine phosphorylation and glycerol exchange across skeletal muscle in lean and obese subjects: effect of beta-adrenergic stimulation
Diabetes
57
1834-1841
2008
Homo sapiens
Manually annotated by BRENDA team
Krintel, C.; Osmark, P.; Larsen, M.R.; Resjoe, S.; Logan, D.T.; Holm, C.
Ser649 and Ser650 are the major determinants of protein kinase A-mediated activation of human hormone-sensitive lipase against lipid substrates
PLoS ONE
3
e3756
2008
Homo sapiens, Homo sapiens (Q05469)
Manually annotated by BRENDA team
Minkkilä, A.; Savinainen, J.; Käsnänen, H.; Xhaard, H.; Nevalainen, T.; Laitinen, J.; Poso, A.; Leppänen, J.; Saario, S.
Screening of various hormone-sensitive lipase inhibitors as endocannabinoid-hydrolyzing enzyme inhibitors
ChemMedChem
4
1253-1259
2009
Homo sapiens
Manually annotated by BRENDA team
Rodriguez, J.; Ben Ali, Y.; Abdelkafi, S.; Mendoza, L.; Leclaire, J.; Fotiadu, F.; Buono, G.; Carrière, F.; Abousalham, A.
In vitro stereoselective hydrolysis of diacylglycerols by hormone-sensitive lipase
Biochim. Biophys. Acta
1801
77-83
2010
Homo sapiens
Manually annotated by BRENDA team
Tanigawa, K.; Degang, Y.; Kawashima, A.; Akama, T.; Yoshihara, A.; Ishido, Y.; Makino, M.; Ishii, N.; Suzuki, K.
Essential role of hormone-sensitive lipase (HSL) in the maintenance of lipid storage in Mycobacterium leprae-infected macrophages
Microb. Pathog.
52
285-291
2012
Homo sapiens
Manually annotated by BRENDA team
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