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1,2-dioleoyl-sn-glycerol + H2O
2-oleoylglycerol + oleate
-
-
-
-
?
1,2-dioleoyl-sn-glycerol + H2O
2-oleylglycerol + oleate
1,2-dioleoyl-sn-glycerol + H2O
?
1,2-dioleoylglycerol + H2O
2-oleoylglycerol + oleate
-
-
mayor end product of trioleoylglycerol and 1,2-dioleoylglycerol hydrolysis
-
?
1-monooleoylglycerol + H2O
glycerol + oleate
-
3times higher activity than with 2-oleoylglycerol
-
-
?
1-myristoyl-2-oleoyl-3-palmitoyl glycerol + H2O
myristate + oleate + palmitate + ?
Halalkalibacterium halodurans
racemic substrate
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
2-monooleoylglycerol + H2O
glycerol + oleate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-nitrophenol caprylate + H2O
4-nitrophenol + caprylate
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl butyrate + H2O
?
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
4-nitrophenyl caproate + H2O
?
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
4-nitrophenyl oleate + H2O
4-nitrophenol + oleate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
Halalkalibacterium halodurans
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
best substrate
-
-
?
alpha-naphtyl acetate + H2O
?
-
-
-
-
?
cholesterol oleate + H2O
cholesterol + oleate
-
-
-
-
?
cholesteryl ester + H2O
cholesterol + a carboxylate
cholesteryl oleate + H2O
?
-
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
cholesteryl oleate + H2O
cholesterol + oleic acid
-
-
-
-
?
coconut oil + H2O
laurate + ?
Halalkalibacterium halodurans
-
-
-
?
cod liver oil + H2O
oleate + ?
Halalkalibacterium halodurans
-
-
-
?
dehydroepiandrosterone oleate + H2O
dehydroepiandrosterone + oleate
-
12.9% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
diacylglycerol + H2O
monoacylglycerol + a carboxylate
dilinolein + H2O
monolineoylglycerol + linoleate
dioleoyl glycerol + H2O
monooleoylglycerol + oleate
-
21% of activity with vinylbutyrate
-
-
?
dioleoylglycerol + H2O
monooleoylglycerol + oleate
-
-
-
-
?
dioleoylglycerol + H2O
oleoylglycerol + oleate
-
-
-
-
?
dipalmitin + H2O
monopalmitoylglycerol + palmitate
dipalmitolein + H2O
monopalmitoleoylglycerol + palmitoleate
distearin + H2O
monostearoylglycerol + stearate
estradiol-17-beta-oleate + H2O
17-beta-estradiol + oleate
-
17.9% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
estradiol-17-beta-palmitate + H2O
17-beta-estradiol + palmitate
-
18.3% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
lipid emulsion + H2O
fatty acids
monoacylglycerol + H2O
glycerol + a carboxylate
oleoylglycerol + H2O
glycerol + oleate
-
-
-
-
?
olive oil + H2O
?
-
3% of activity with vinylbutyrate
-
-
?
p-nitrophenyl acetate + H2O
?
using various p-nitrophenyl esters as substrates. Enzyme efficiently hydrolyzes p-nitrophenyl acetate (75%), p-nitrophenyl butyrate (100%), p-nitrophenyl carproate (55%) and p-nitrophenyl caprylate (50%), a lower level of hydrolysis is observed for p-nitrophenyl decanoate (25%), p-nitrophenyl palmitate (2%) and p-nitrophenyl stearate (2%)
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
?
using various p-nitrophenyl esters as substrates. Enzyme efficiently hydrolyzes p-nitrophenyl acetate (75%), p-nitrophenyl butyrate (100%), p-nitrophenyl carproate (55%) and p-nitrophenyl caprylate (50%), a lower level of hydrolysis is observed for p-nitrophenyl decanoate (25%), p-nitrophenyl palmitate (2%) and p-nitrophenyl stearate (2%)
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
p-nitrophenyl caproate + H2O
?
using various p-nitrophenyl esters as substrates. Enzyme efficiently hydrolyzes p-nitrophenyl acetate (75%), p-nitrophenyl butyrate (100%), p-nitrophenyl carproate (55%) and p-nitrophenyl caprylate (50%), a lower level of hydrolysis is observed for p-nitrophenyl decanoate (25%), p-nitrophenyl palmitate (2%) and p-nitrophenyl stearate (2%)
-
-
?
p-nitrophenyl caprylate + H2O
?
using various p-nitrophenyl esters as substrates. Enzyme efficiently hydrolyzes p-nitrophenyl acetate (75%), p-nitrophenyl butyrate (100%), p-nitrophenyl carproate (55%) and p-nitrophenyl caprylate (50%), a lower level of hydrolysis is observed for p-nitrophenyl decanoate (25%), p-nitrophenyl palmitate (2%) and p-nitrophenyl stearate (2%)
-
-
?
p-nitrophenyl decanoate + H2O
?
using various p-nitrophenyl esters as substrates. Enzyme efficiently hydrolyzes p-nitrophenyl acetate (75%), p-nitrophenyl butyrate (100%), p-nitrophenyl carproate (55%) and p-nitrophenyl caprylate (50%), a lower level of hydrolysis is observed for p-nitrophenyl decanoate (25%), p-nitrophenyl palmitate (2%) and p-nitrophenyl stearate (2%)
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
SsoNDELTAlong, is 15fold more active with the substrate p-nitrophenyl hexanoate than SsoNDELTA
-
-
?
p-nitrophenyl laurate + H2O
p-nitrophenol + laurate
-
-
-
-
?
p-nitrophenyl palmitate + H2O
?
using various p-nitrophenyl esters as substrates. Enzyme efficiently hydrolyzes p-nitrophenyl acetate (75%), p-nitrophenyl butyrate (100%), p-nitrophenyl carproate (55%) and p-nitrophenyl caprylate (50%), a lower level of hydrolysis is observed for p-nitrophenyl decanoate (25%), p-nitrophenyl palmitate (2%) and p-nitrophenyl stearate (2%)
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
-
-
-
-
?
p-nitrophenyl stearate + H2O
?
using various p-nitrophenyl esters as substrates. Enzyme efficiently hydrolyzes p-nitrophenyl acetate (75%), p-nitrophenyl butyrate (100%), p-nitrophenyl carproate (55%) and p-nitrophenyl caprylate (50%), a lower level of hydrolysis is observed for p-nitrophenyl decanoate (25%), p-nitrophenyl palmitate (2%) and p-nitrophenyl stearate (2%)
-
-
?
p-nitrophenyl-dodecanoate + H2O
p-nitrophenol + dodecanoate
SsoNDELTA shows 4.4fold lower activity than SsoNDELTAlong with p-nitrophenyl-dodecanoate as substrate
-
-
?
palm oil + H2O
palmitate + ?
Halalkalibacterium halodurans
-
-
-
?
rac 1,2(2,3)-sn diolein + H2O
?
-
-
-
-
?
testosterone oleate + H2O
testosterone + oleate
-
1.4% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
tributanoyl glycerol + H2O
dibutanoylglycerol + butanoate
-
8% of activity with vinylbutyrate
-
-
?
tributanoylglycerol + H2O
dibutanoylglycerol + butanoate
-
-
-
-
?
tributyrin + H2O
dibutanoylglycerol + butanoate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
tributyrylglycerol + H2O
?
SsoNDELTA shows 6old lower activity than SsoNDELTAlong with glyceryl tributyrate as substrate
-
-
?
tricaproyl glycerol + H2O
dicaproyl glycerol + caprate
Halalkalibacterium halodurans
-
-
-
?
tridecanoylglycerol + H2O
?
SsoNDELTA shows 4.7fold higher activity than SsoNDELTAlong with glyceryl tridecanoate as substrate
-
-
?
trihexadecenoin + H2O
dihexadecenoin + hexadecenoate
trihexanoylglycerol + H2O
?
SsoNDELTA shows 4fold lower activity than SsoNDELTAlong with glyceryl trihexanoate as substrate
-
-
?
trilinolein + H2O
1,2-dilinoleoylglycerol + oleate
complete conversion
-
-
?
trioctanoin + H2O
dioctanoylglycerol + octanoate
-
-
-
-
?
trioctanoyl glycerol + H2O
dioctanoylglycerol + octanoate
-
3% of activity with vinylbutyrate
-
-
?
trioctanoylglycerol + H2O
?
SsoNDELTA shows 1.7fold lower activity than SsoNDELTAlong with glyceryl trioctanoate as substrate
-
-
?
triolein + H2O
1,2-dioleoylglycerol + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
triolein + H2O
dioleoylglycerol + oleate
trioleoyl glycerol + H2O
dioleoyl glycerol + oleate
Halalkalibacterium halodurans
-
-
-
?
trioleoylglycerol + H2O
1,2-dioleoylglycerol + oleate
-
-
-
-
?
trioleoylglycerol + H2O
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
tripalmitin + H2O
1,2-dipalmitoylglycerol + palmitate
complete conversion
-
-
?
tripalmitoyl glycerol + H2O
dipalmitoyl glycerol + palmitate
Halalkalibacterium halodurans
-
-
-
?
tripropionin + H2O
dipropanoylglycerol + propanoate
-
-
-
-
?
tripropionyl glycerol + H2O
dipropionylglycerol + propionate
-
4% of activity with vinylbutyrate
-
-
?
tristearin + H2O
1,2-distearoylglycerol + stearate
complete conversion
-
-
?
vinyl acetate + H2O
acetate + ethylenol
-
-
-
-
?
vinyl acetate + H2O
vinyl alcohol + acetate
-
67% of activity with vinylbutyrate
-
-
?
vinyl butyrate + H2O
butanoate + ethylenol
-
-
-
-
?
vinyl butyrate + H2O
vinyl alcohol + butanoate
-
-
-
-
?
vinyl laurate + H2O
laurate + ethylenol
-
-
-
-
?
vinyl laurate + H2O
vinyl alcohol + laurate
-
15% of activity with vinylbutyrate
-
-
?
vinyl propionate + H2O
propanoate + ethylenol
-
-
-
-
?
vinyl propionate + H2O
vinyl alcohol + propionate
-
50% of activity with vinylbutyrate
-
-
?
additional information
?
-
1,2-dioleoyl-sn-glycerol + H2O
2-oleylglycerol + oleate
-
-
-
-
?
1,2-dioleoyl-sn-glycerol + H2O
2-oleylglycerol + oleate
-
-
-
-
?
1,2-dioleoyl-sn-glycerol + H2O
2-oleylglycerol + oleate
-
-
-
-
?
1,2-dioleoyl-sn-glycerol + H2O
?
-
-
-
?
1,2-dioleoyl-sn-glycerol + H2O
?
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
4-nitrophenol caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenol caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenol caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
high activity
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Halalkalibacterium halodurans
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Halalkalibacterium halodurans DSM 18197
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
high activity
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
Halalkalibacterium halodurans
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
low activity
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Halalkalibacterium halodurans
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Halalkalibacterium halodurans DSM 18197
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
low activity
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
Halalkalibacterium halodurans
best substrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
Halalkalibacterium halodurans DSM 18197
best substrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
low activity
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
Halalkalibacterium halodurans
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
Halalkalibacterium halodurans DSM 18197
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
Halalkalibacterium halodurans
70% of the activity with 4-nitrophenyl laurate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
Halalkalibacterium halodurans DSM 18197
70% of the activity with 4-nitrophenyl laurate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
low activity
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
-
?
cholesteryl ester + H2O
cholesterol + a carboxylate
-
-
-
-
?
cholesteryl ester + H2O
cholesterol + a carboxylate
-
overexpression of HSL increases the supply of free cholesterol as a ligand for liver X receptor, thereby stimulates the expression of ABCA1 gene in macrophages
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
-
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
18.5% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
-
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
-
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
-
approx. 55% of activity with dioleoylglcerol
-
-
?
diacylglycerol + H2O
monoacylglycerol + a carboxylate
-
-
-
-
?
diacylglycerol + H2O
monoacylglycerol + a carboxylate
-
-
-
-
?
diacylglycerol + H2O
monoacylglycerol + a carboxylate
-
-
-
-
?
diacylglycerol + H2O
monoacylglycerol + a carboxylate
-
-
-
-
?
dilinolein + H2O
monolineoylglycerol + linoleate
complete conversion
-
-
?
dilinolein + H2O
monolineoylglycerol + linoleate
over 50% conversion
-
-
?
dilinolein + H2O
monolineoylglycerol + linoleate
complete conversion
-
-
?
dilinolein + H2O
monolineoylglycerol + linoleate
over 50% conversion
-
-
?
dilinolein + H2O
monolineoylglycerol + linoleate
complete conversion
-
-
?
dilinolein + H2O
monolineoylglycerol + linoleate
over 50% conversion
-
-
?
dipalmitin + H2O
monopalmitoylglycerol + palmitate
complete conversion
-
-
?
dipalmitin + H2O
monopalmitoylglycerol + palmitate
complete conversion
-
-
?
dipalmitin + H2O
monopalmitoylglycerol + palmitate
complete conversion
-
-
?
dipalmitolein + H2O
monopalmitoleoylglycerol + palmitoleate
complete conversion
-
-
?
dipalmitolein + H2O
monopalmitoleoylglycerol + palmitoleate
over 50% conversion
-
-
?
dipalmitolein + H2O
monopalmitoleoylglycerol + palmitoleate
complete conversion
-
-
?
dipalmitolein + H2O
monopalmitoleoylglycerol + palmitoleate
over 50% conversion
-
-
?
dipalmitolein + H2O
monopalmitoleoylglycerol + palmitoleate
complete conversion
-
-
?
dipalmitolein + H2O
monopalmitoleoylglycerol + palmitoleate
over 50% conversion
-
-
?
distearin + H2O
monostearoylglycerol + stearate
complete conversion
-
-
?
distearin + H2O
monostearoylglycerol + stearate
over 50% conversion
-
-
?
distearin + H2O
monostearoylglycerol + stearate
over 50% conversion
-
-
?
distearin + H2O
monostearoylglycerol + stearate
complete conversion
-
-
?
distearin + H2O
monostearoylglycerol + stearate
over 50% conversion
-
-
?
distearin + H2O
monostearoylglycerol + stearate
complete conversion
-
-
?
lipid emulsion + H2O
fatty acids
-
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
-
?
lipid emulsion + H2O
fatty acids
-
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
-
?
monoacylglycerol + H2O
glycerol + a carboxylate
-
-
-
-
?
monoacylglycerol + H2O
glycerol + a carboxylate
-
-
-
-
?
monoacylglycerol + H2O
glycerol + a carboxylate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
trihexadecenoin + H2O
dihexadecenoin + hexadecenoate
complete conversion
-
-
?
trihexadecenoin + H2O
dihexadecenoin + hexadecenoate
below 30% conversion
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
dioleoylglycerol + oleate
-
-
-
-
?
triolein + H2O
dioleoylglycerol + oleate
-
-
-
-
?
triolein + H2O
dioleoylglycerol + oleate
-
-
-
-
?
triolein + H2O
dioleoylglycerol + oleate
-
-
-
-
?
trioleoylglycerol + H2O
?
-
-
-
?
trioleoylglycerol + H2O
?
SsoNDELTA shows 10fold higher activity than SsoNDELTAlong with glyceryl trioleate as substrate
-
-
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
-
-
-
-
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
-
-
-
-
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
-
approx. 16% of activity with dioleoylglcerol
-
-
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
-
the type of dietary fat has no effect on kinetic properties of hormone-sensitive lipase
-
-
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
-
-
-
-
?
trioleoylglycerol + H2O
dioleoylglycerol + oleate
-
suspended in glycerol/phospholipid, 30-50% of a gum-based substrate suspension
-
-
?
additional information
?
-
no activity with chain length exceeding C6
-
-
?
additional information
?
-
-
no activity with chain length exceeding C6
-
-
?
additional information
?
-
-
hormone-sensitive lipase may be the rate-limiting enzyme controlling the cellular catabolism of diacylglycerol in adipose tissue and that of cholesteryl esters in macrophage foam cells and steroidogenic tissues releasing the cholesterol required for adrenal steroidogenesis
-
-
?
additional information
?
-
-
in the skeletal muscle at rest there is a high constitutive level of hormone-sensitive lipase activity, which is not a function of biopsy freezing. The combination of low adrenaline and Ca2+ levels and resting levels of insulin appears to dictate the levels of activity of hormone-sensitive lipase at rest. During the onset of low and moderate aerobic exercise enzyme activity is activated by contractions, in the apparent absence of increases in circulating adrenaline. However, adrenaline may contribute to the early activation of the enzyme during intense aerobic exercise. The contraction-induced activation appears to be related to the increase in protein kinase C and extracellular signal regulated kinase activity associated with Ca2+ and/or other unknown activators. As low- and moderate-intensity exercise continues beyond a few min, activation by adrenaline through the cAMP cascade and protein kinase A also appears to occur. With prolonged moderate-intensity exercise beyond 1–2 h and sustained high-intensity exercise, HSL activity decreases despite continuing increases in adrenaline, possibly as a result of increasing accumulation of free AMP, activation of AMP-activated kinase and phosphorylation of inhibitory sites on the hormone-sensitive lipase. Intramuscular factors dominate the control of hormone-sensitive lipase activity, with hormonal factors playing a smaller role
-
-
?
additional information
?
-
-
the enzyme catalyses the hydrolysis of myocellular triacylglycerol, which is a potential energy source diuring exercise
-
-
?
additional information
?
-
-
the enzyme is involved in the hormone regulated release of fatty acids and glycerol from adipocyte lipid stores
-
-
?
additional information
?
-
-
the enzyme a substrate preference for the diacylglycerols originating from triacylglycerols. The ee% of 1,2-sn-diolein over 2,3-sn-diolein increases with the level of hydrolysis indicated that HSL has a preference for 2,3-sn-diolein as a substrate and therefore a stereopreference for the sn-3 position of dioleoylglycerol. The ee% of 1,2-sn-diolein reaches a maximum value of 36% at 42% hydrolysis
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity of enzyme Lip1 with tristearin, trilinolein, and tripalmitoylglycerol. Lip1 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
no activity with dipalmitin, MDL2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip2 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
Lip3 substrate specificity, overview
-
-
?
additional information
?
-
-
hormone-sensitive lipase is required for high-density lipoprotein cholesteryl ester-supported adrenal steroidogenesis
-
-
?
additional information
?
-
hormone-sensitive lipase is a key enzyme of acylglycerol metabolism in white adipose tissue. The hormone-sensitive lipase activity in white adipose tissue is important for metabolic plasticity and inflammation. Hormone-sensitive lipase-mediated lipolysis and subsequent downstream free fatty acid signaling are important components of adipose tissue remodeling following acute and chronic beta3-adrenergic receptor activation
-
-
?
additional information
?
-
-
hypothesis that HSL functions as a cholesterol ester hydrolase rather than as a lipase with regard to GSIS and beta-cells
-
-
?
additional information
?
-
-
sn-1,3-diacylglycerol is the preferred substrate for the consecutive hydrolysis by hormone-sensitive lipase, the enzyme is less active with sn-1,2-diacylglycerol
-
-
?
additional information
?
-
-
LIPY may be responsible for the utilization of stored triglycerides during dormancy and reactivation of the pathogen Mycobacterium tuberculosis
-
-
?
additional information
?
-
-
expressed at a higher level in oxidative fibres than in glycolytic fibres. The two physiological stimuli adrenaline and contraction increase enzyme activity in muscle, and the effects are partially additive. Adrenaline acts via beta-adrenergic activation of cAMP-dependent protein kinase, while the effect of contractions is mediated by protein kinase C, at least partly via the extracellular signal-regulated kinase pathway. Endurance training diminishes the sensitivity of muscle hormone-sensitive lipase to adrenaline but increases the contraction-mediated activation
-
-
?
additional information
?
-
key enzyme in fatty acid mobilization
-
-
?
additional information
?
-
-
rate-limiting enzyme in lipolysis
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity, with a strong preference towards short-chain esters, e.g. 4-nitrophenyyl acetateand 4-nitrophenyyl butyrate, little activity is observed towards long-chain esters such as 4-nitrophenyl dodecanoate
-
-
?
additional information
?
-
Est22 hydrolyzes 4-nitrophenyl esters up to C8, while the enzymatic activity decreases significantly with increasing chain length
-
-
?
additional information
?
-
the purified enzyme Est06 exhibits high affinity for acyl esters with short-chain fatty acids, and shows optimum activity with p-nitrophenyl valerate
-
-
?
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(3,4-dihydro-1H-isoquinolin-2-yl)-carbamic acid 4-tert-butoxycarbonylamino-phenyl ester
-
IC50: 3 nM
(5-chloro-2-[([6-[4-(trifluoromethyl)phenoxy]pyridin-3-yl]carbonyl)amino]phenyl)boronic acid
-
potent HSL inhibitor with a significantly reduced bioactivation potential. Oral administration of compound exhibit an antilipolytic effect on rats at 3 mg/kg
(5-fluoro-2-[([6-[4-(trifluoromethyl)phenoxy]pyridin-3-yl]carbonyl)amino]phenyl)boronic acid
-
potent inhibitor, in vitro and in cell with high selectivity for cholinesterases AChE and BuChE. The compound exhibits antilipolytic effect in rats at 1 mg/kg p.o. and does not show bioactivation
(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
2-propanol
-
80-90% inhibition
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-chloromercuribenzoate
-
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
76-0079
-
a commercial small molecule inhibitor
-
Ba2+
10 mM, 40% loss of activity
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
betaine
-
it enhances the enzyme activity 2fold at 50°C and 3 M, and 1.5fold at 45°C and 1-3 M, while it reduces the enzyme activity at 35-40°C, by 20% at 40°C and 3 M,about % at 1 M, overview
CaCl2
-
50 mM, 47% inhibition
Co2+
45% inhibition at 1 mM
CoCl2
-
10 mM, 34% inhibition
Diethyl p-nitrophenyl phosphate
-
100fold molar excess, complete inactivation after 15 min
diethyl-p-nitrophenyl phosphate
-
0.1 mM, 94% inhibition
diisopropyl fluorophosphate
diisopropylfluorophosphate
DMSO
increase in enzyme activity (130%) is observed at 25% v/v DMSO although at a higher concentration (50%), DMSO decreases enzyme activity to 72%
Emulgen 120
-
0.1%, 955 of cholesteryl oleate hydrolysis
ethanol
-
80-90% inhibition
ethyl (4-[[(morpholin-4-ylamino)carbonyl]oxy]phenyl)acetate
-
IC50: 138 nM
Fe2+
35% inhibition at 1 mM
L-cysteine
-
inhibits the enzyme activity in presence of TNF-alpha
L-cystine
-
inhibits the enzyme activity in presence of TNF-alpha
L-methionine
-
L-methionine enhances the enzyme activaty in absence of tumor necrosis factor-alpha, but inhibits it in presence of TNF-alpha
methanol
-
80-90% inhibition
methyl 2-(hexadecyloxy)-4-methyl-6,7-dihydro-1,3,2-dioxaphosphepine-5-carboxylate 2-oxide
-
-
methyl 4-[[(3,4-dihydroisoquinolin-2(1H)-ylamino)carbonyl]oxy]benzoate
-
IC50: 9952 nM
MgCl2
-
50 mM, 52% inhibition
MnCl2
-
50 mM, 45% inhibition
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
NaCl
0.1 M, 90% residual activity, 1 M, 30% residual activity
Ni2+
10 mM, 50% loss of activity
Pb2+
Halalkalibacterium halodurans
5 mM, 65% residual activity
phenyl 3,4-dihydroisoquinolin-2(1H)-ylcarbamate
-
IC50: 205 nM
phenylmethanesulfonyl fluoride
-
0.01 mM, approx. 75% inhibition, 0.01 mM, approx. 90% inhibition
phenylmethylsulfonyl fluoride
-
100fold molar excess, complete inactivation after 15 min
proline
-
inhibits the enzyme at 35-50°C and concentrations of 1-3 M
trans-cyclipostin P
-
irreversible
Trimethylamine N-oxide
-
it enhances the enzyme activity 2.5fold at 50°C and 3 M, and 5fold at 45°C and 1 M, while it reduces the enzyme activity at 35-40°C, by 60% at 40°C and 3 M, 10% at 1 M, overview
Triton X-100
-
above 0.1%
Zn2+
10 mM, complete loss of activity
ZnCl2
-
44% inhibition at 10 mM, 99% inhibition at 50 mM
CAY10499
in periparturient dairy cows, the compound inhibits basal lipolysis negligibly at 11 d prepartum, but at 11 and 24 d postpartum it reduces basal lipolysis by 36.1% and 43.1%, respectively
Cu2+
-
10 mM, 50-60% inhibition
Cu2+
10 mM, complete loss of activity
diisopropyl fluorophosphate
-
complete inhibition
diisopropyl fluorophosphate
-
serine hydrolase, active-site at position 424
diisopropyl fluorophosphate
-
0.1 mM, 92% inhibition
diisopropyl fluorophosphate
-
serine hydrolase with the active-site serine at position 423
diisopropyl fluorophosphate
-
0.1 mM, 98% inhibition
diisopropylfluorophosphate
-
0.012 mM, 50% inhibition after 30 min incubation
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
0.1 mM, 98% inhibition
diisopropylfluorophosphate
-
diisopropylfluorophosphate
-
0.0075 mM, 50% inhibition
Hg2+
-
0.005 mM, approx. 50% inhibition, 0.02 mM, approx. 70% inhibition
Hg2+
-
0.1 mM, 91% inhibition
Hg2+
-
0.1 mM, complete inhibition
Hg2+
-
0.1 mM, 96% inhibition
Hg2+
-
10 mM, 50-60% inhibition
HgCl2
-
0.1 mM, 93% inhibition
HgCl2
-
0.01 mM, 50% inhibition
NaF
-
20 mM, 50% inhibition of p-nitrophenyl butyrate hydrolysis, 70% of triolein hydrolysis, 60% of cholesteryl hydrolysis
NaF
-
100 mM, 67% inhibition
NaF
-
0.1 mM, 91% inhibition
NaF
-
0.1 mM, 90% inhibition
NaF
-
4 mM, 50% inhibition
PMSF
Halalkalibacterium halodurans
5 mM, 17% residual activity
SDS
Halalkalibacterium halodurans
5 mM, 63% residual activity
SDS
-
above 2 mM. Inhibition by SDS is partially reversed by Triton X-100
SDS
1%, complete loss of activity
SDS
complete inactivation
Tween 20
-
inhibits from 0.1 to 2.0%
additional information
insulin (5-10 ng/ml) induces down-regulation of HSL, dexamethasone (50–250 nM) induces down-regulation of HSL, bovine growth hormone (50 ng/ml) induces down-regulation of HSL
-
additional information
-
insulin (5-10 ng/ml) induces down-regulation of HSL, dexamethasone (50–250 nM) induces down-regulation of HSL, bovine growth hormone (50 ng/ml) induces down-regulation of HSL
-
additional information
Halalkalibacterium halodurans
not inhibitory: EDTa or EGTA, dithiothreitol at 5 mM
-
additional information
hormone-sensitive lipase is knocked down by RNA interference or selectively inhibited
-
additional information
-
hormone-sensitive lipase is knocked down by RNA interference or selectively inhibited
-
additional information
-
incubation with LDL augments the accumulation of cholesteryl ester in the HSL-deficient hepatocytes
-
additional information
-
polyunsaturated species of triacylglycerols containing 18:2 or 20:4 double bonds depress rates of oleate release by 70-75% below control values
-
additional information
no inhibition by EDTA, poor effect by Triton X-100
-
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evolution
phylogentic analysis suggests that the two HSL isozymes derive from paralogous genes that may have arisen during a teleost-specific genome duplication event
evolution
archaeon Sulfolobus solfataricus P1 carboxylesterase is a thermostable enzyme belonging to the mammalian hormone-sensitive lipase (HSL) family. Enzyme SsoP1Est belongs to the HSL family exhibiting a classic alpha/beta hydrolase fold by sequence alignment with homologous esterases, which were well characterized in the structure. Thus, it contains a typical catalytic triad of esterases, which is expected to be composed of Ser151, Asp244, and His274, and another typical oxyanion hole, which is presumed to be composed of Gly80, Gly81, and Ala152
evolution
Lip1 is a family class 3 lipase. Family class 3 lipases are specific for mono- and diacylglycerols, but exhibit no regioselective production of diacylglycerols, in Malassezia globosa only LIP family lipases show activity on triacylglycerides. Comparisons of sequences and structures of Malassezia globosa lipases, overview
evolution
Lip1 is a family class LIP lipase. Family class 3 lipases are specific for mono- and diacylglycerols, but exhibit no regioselective production of diacylglycerols, in Malassezia globosa only LIP family lipases show activity on triacylglycerides. Comparisons of sequences and structures of Malassezia globosa lipases, overview
evolution
the enzyme is a metagenome-derived member of the hormone-sensitive lipase family of lipolytic enzymes
evolution
-
archaeon Sulfolobus solfataricus P1 carboxylesterase is a thermostable enzyme belonging to the mammalian hormone-sensitive lipase (HSL) family. Enzyme SsoP1Est belongs to the HSL family exhibiting a classic alpha/beta hydrolase fold by sequence alignment with homologous esterases, which were well characterized in the structure. Thus, it contains a typical catalytic triad of esterases, which is expected to be composed of Ser151, Asp244, and His274, and another typical oxyanion hole, which is presumed to be composed of Gly80, Gly81, and Ala152
-
evolution
-
Lip1 is a family class 3 lipase. Family class 3 lipases are specific for mono- and diacylglycerols, but exhibit no regioselective production of diacylglycerols, in Malassezia globosa only LIP family lipases show activity on triacylglycerides. Comparisons of sequences and structures of Malassezia globosa lipases, overview
-
evolution
-
Lip1 is a family class LIP lipase. Family class 3 lipases are specific for mono- and diacylglycerols, but exhibit no regioselective production of diacylglycerols, in Malassezia globosa only LIP family lipases show activity on triacylglycerides. Comparisons of sequences and structures of Malassezia globosa lipases, overview
-
evolution
-
archaeon Sulfolobus solfataricus P1 carboxylesterase is a thermostable enzyme belonging to the mammalian hormone-sensitive lipase (HSL) family. Enzyme SsoP1Est belongs to the HSL family exhibiting a classic alpha/beta hydrolase fold by sequence alignment with homologous esterases, which were well characterized in the structure. Thus, it contains a typical catalytic triad of esterases, which is expected to be composed of Ser151, Asp244, and His274, and another typical oxyanion hole, which is presumed to be composed of Gly80, Gly81, and Ala152
-
evolution
-
Lip1 is a family class 3 lipase. Family class 3 lipases are specific for mono- and diacylglycerols, but exhibit no regioselective production of diacylglycerols, in Malassezia globosa only LIP family lipases show activity on triacylglycerides. Comparisons of sequences and structures of Malassezia globosa lipases, overview
-
evolution
-
Lip1 is a family class LIP lipase. Family class 3 lipases are specific for mono- and diacylglycerols, but exhibit no regioselective production of diacylglycerols, in Malassezia globosa only LIP family lipases show activity on triacylglycerides. Comparisons of sequences and structures of Malassezia globosa lipases, overview
-
malfunction
-
depletion of the enzyme affects lipoprotein-derived cellular cholesterol influx, diminishes the supply of cholesterol to the mitochondria, and results in the repression of steroidogenic acute regulatory protein and phospho-steroidogenic acute regulatory protein levels
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
malfunction
-
enzyme-deficient mice accumulate sn-1,3-diacylglycerol and sn-2,3-diacylglycerol in white adipose tissue
malfunction
-
in male mice, deficiency of hormone sensitive lipase causes deficient spermatogenesis, azoospermia, and infertility
malfunction
-
enzyme-deficient mice accumulate sn-1,3-diacylglycerol and sn-2,3-diacylglycerol in white adipose tissue
-
malfunction
-
depletion of the enzyme affects lipoprotein-derived cellular cholesterol influx, diminishes the supply of cholesterol to the mitochondria, and results in the repression of steroidogenic acute regulatory protein and phospho-steroidogenic acute regulatory protein levels
-
physiological function
-
acute exercise has an effect on lipolysis via coordination of hormone-sensitive lipase and scaffold proteins, i.e., perilipin A and comparative gene identification-58, i.e. CGI-58, in rat primary adipocyte leading to increased glycerol release immediately after exercise, overview
physiological function
-
hormone-sensitive lipase contributes importantly to the mobilization of fatty acids in adipocytes and shows a substrate preference for the diacylglycerols originating from triacylglycerols
physiological function
-
hormone-sensitive lipase modulates adipose metabolism by providing intrinsic ligands or pro-ligands for PPARgama, mechanism, overview
physiological function
-
hormone-sensitive lipase regulates triglycerides breakdown under hormonal control. Left ventricle HSL activity against triglycerides is significantly elevated in intact rats supplemented with testosterone
physiological function
-
key enzyme in fatty acid mobilization and lipolysis
physiological function
-
the catalytic function of hormone-sensitive lipase is essential for spermatogenesis in male mice, while the presence of the enzyme's N-terminal testis-specific fragment is not essential
physiological function
-
the enzyme is crucial for the hydrolysis of diacylglycerol within the lipolytic cascade
physiological function
-
the enzyme is primarily involved in catalyzing cholesteryl ester hydrolysis and plays an important role in the regulation of cAMP-mediated steroidogenic acute regulatory protein expression and steroidogenesis through modulation of liver X receptor pathways. The enzyme-dependent regulation of steroidogenesis predominantly involves liver X recetor signaling. Enzyme-mediated steroidogenesis entails enhanced oxysterol production. Hormonal control of the enzyme activity is primarily mediated by the phosphorylation of serine residues, Ser563, Ser659, and Ser660
physiological function
-
adipose triglyceride lipase Atgl and hormone-sensitive lipase Hsl mRNA expression is time-dependently increased by fasting, along with other fatty acid metabolism genes (Pparx02, Cd36, and Aox). ATGL and HSL protein levels are induced by 239 and 322%, respectively. There is an increase in ATGL phosphorylation at the AMPK-regulated serine 406 site in the 14-3-3 binding motif, and an increase in HSL phosphorylation at serines 565 and 660 that are regulated by AMPK and PKA, respectively
physiological function
HSL contribution to basal lipolysis is negligible prepartum in periparturient dairy cows. HSL is a major driver of subcutaneous adipose tissue lipolytic responses postpartum. Reduced lipogenesis is an important contributor to fatty acid release from subcutaneous adipose tissue
physiological function
hyperleptinemia equally suppresses the food intake in wild-type and Hsl KO mice. Leptin-mediated fat loss and glucose-lowering are significantly blunted in the absence of HSL when leptin is overexpressed by recombinant adenovirus carrying leptin. Hsl KO mice have a tendency to retain more fat than wild-type mice in the face of hyperleptinemia
physiological function
in human skeletal muscle in vivo HSL preferentially redistributes to peripilin PLIN5-associated lipid droplets with moderate-intensity exercise
physiological function
the enzyme plays a potential role in colonizing human skin
physiological function
-
hormone-sensitive lipase modulates adipose metabolism by providing intrinsic ligands or pro-ligands for PPARgama, mechanism, overview
-
physiological function
-
the enzyme is crucial for the hydrolysis of diacylglycerol within the lipolytic cascade
-
physiological function
-
the enzyme plays a potential role in colonizing human skin
-
physiological function
-
acute exercise has an effect on lipolysis via coordination of hormone-sensitive lipase and scaffold proteins, i.e., perilipin A and comparative gene identification-58, i.e. CGI-58, in rat primary adipocyte leading to increased glycerol release immediately after exercise, overview
-
physiological function
-
the enzyme is primarily involved in catalyzing cholesteryl ester hydrolysis and plays an important role in the regulation of cAMP-mediated steroidogenic acute regulatory protein expression and steroidogenesis through modulation of liver X receptor pathways. The enzyme-dependent regulation of steroidogenesis predominantly involves liver X recetor signaling. Enzyme-mediated steroidogenesis entails enhanced oxysterol production. Hormonal control of the enzyme activity is primarily mediated by the phosphorylation of serine residues, Ser563, Ser659, and Ser660
-
physiological function
-
the enzyme plays a potential role in colonizing human skin
-
additional information
-
hormone-sensitive lipase is significantly increased in white adipose tissue of fasted JunB-KO mice, after JunB silencing through knockdown via lentiviruses harboring a shRNA construct targeted against JunB, the effect might be due to a systemic effect/factor in JunB-KO mice, like the significantly decreased insulin levels, metbaolic phenotype, overview
additional information
the organism possesses two hormone-sensitive lipase-encoding mRNAs that are differentially expressed and independently regulated by nutritional state
additional information
the organism possesses two hormone-sensitive lipase-encoding mRNAs that are differentially expressed and independently regulated by nutritional state
additional information
-
the organism possesses two hormone-sensitive lipase-encoding mRNAs that are differentially expressed and independently regulated by nutritional state
additional information
-
cells deficient in liver X receptors exhibit decreased enzyme responsiveness
additional information
the enzyme contains a catalytic Ser201 and the other two catalytic residues Asp303 and His333, that perfectly match to corresponding residues in proteins within the HSL family
additional information
-
the hormone-sensitive lipase catalyzes the hydrolysis of fatty acid esters at very low temperature and is extremely active
additional information
catalytic residues are Asp28 and His281
additional information
catalytic residues are Asp28 and His281
additional information
catalytic residues are Asp28 and His281
additional information
catalytic residues are Asp28 and His281
additional information
-
catalytic residues are Asp28 and His281
additional information
catalytic residues are Asp44 and His378
additional information
catalytic residues are Asp44 and His378
additional information
catalytic residues are Asp44 and His378
additional information
catalytic residues are Asp44 and His378
additional information
-
catalytic residues are Asp44 and His378
additional information
catalytic residues are Ser197, Asp44, and His378
additional information
catalytic residues are Ser197, Asp44, and His378
additional information
catalytic residues are Ser197, Asp44, and His378
additional information
catalytic residues are Ser197, Asp44, and His378
additional information
-
catalytic residues are Ser197, Asp44, and His378
additional information
Est06 has a HGGG motif (residues 74 to 77) and a catalytic triad composed of Ser144, Glu238, and His268
additional information
residues Ser151, Asp244, and His274 form the catalytic triad of the native SsoP1Est, residues Gly80, Gly81, and Ala152 form the oxyanion hole. Enzyme structure homology modeling, overview
additional information
-
residues Ser151, Asp244, and His274 form the catalytic triad of the native SsoP1Est, residues Gly80, Gly81, and Ala152 form the oxyanion hole. Enzyme structure homology modeling, overview
-
additional information
-
the hormone-sensitive lipase catalyzes the hydrolysis of fatty acid esters at very low temperature and is extremely active
-
additional information
-
catalytic residues are Asp28 and His281
-
additional information
-
catalytic residues are Asp44 and His378
-
additional information
-
catalytic residues are Ser197, Asp44, and His378
-
additional information
-
residues Ser151, Asp244, and His274 form the catalytic triad of the native SsoP1Est, residues Gly80, Gly81, and Ala152 form the oxyanion hole. Enzyme structure homology modeling, overview
-
additional information
-
cells deficient in liver X receptors exhibit decreased enzyme responsiveness
-
additional information
-
catalytic residues are Asp28 and His281
-
additional information
-
catalytic residues are Asp44 and His378
-
additional information
-
catalytic residues are Ser197, Asp44, and His378
-
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Homo sapiens, Rattus norvegicus
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Rattus norvegicus
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Homo sapiens
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Mus musculus
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Homo sapiens
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281
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2006
Mus musculus
brenda
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Mus musculus
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Homo sapiens
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Cardiac overexpression of hormone-sensitive lipase inhibits myocardial steatosis and fibrosis in streptozotocin diabetic mice
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294
E1109-E1118
2008
Mus musculus, Mus musculus C57BL/6
brenda
Fernandez, C.; Hansson, O.; Nevsten, P.; Holm, C.; Klint, C.
Hormone-sensitive lipase is necessary for normal mobilization of lipids during submaximal exercise
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295
E179-E186
2008
Homo sapiens (Q05469)
brenda
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2008
Mus musculus
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Yonezawa, T.; Haga, S.; Kobayashi, Y.; Katoh, K.; Obara, Y.
Regulation of hormone-sensitive lipase expression by saturated fatty acids and hormones in bovine mammary epithelial cells
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376
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2008
Bos taurus (P16386), Bos taurus
brenda
Larsson, S.; Wierup, N.; Sundler, F.; Eliasson, L.; Holm, C.
Lack of cholesterol mobilization in islets of hormone-sensitive lipase deficient mice impairs insulin secretion
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376
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2008
Mus musculus
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Nam, K.H.; Kim, M.Y.; Kim, S.J.; Priyadarshi, A.; Lee, W.H.; Hwang, K.Y.
Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase
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379
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2009
uncultured bacterium (Q0GMU2)
brenda
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
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2008
Homo sapiens
brenda
Fex, M.; Haemmerle, G.; Wierup, N.; Dekker-Nitert, M.; Rehn, M.; Ristow, M.; Zechner, R.; Sundler, F.; Holm, C.; Eliasson, L.; Mulder, H.
A beta cell-specific knockout of hormone-sensitive lipase in mice results in hyperglycaemia and disruption of exocytosis
Diabetologia
52
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2009
Mus musculus (P54310), Mus musculus
brenda
Lobo, M.V.; Huerta, L.; Arenas, M.I.; Busto, R.; Lasuncion, M.A.; Martin-Hidalgo, A.
Hormone-sensitive lipase expression and IHC localization in the rat ovary, oviduct, and uterus
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57
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2009
Rattus norvegicus (P15304)
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Sekiya, M.; Osuga, J.; Yahagi, N.; Okazaki, H.; Tamura, Y.; Igarashi, M.; Takase, S.; Harada, K.; Okazaki, S.; Iizuka, Y.; Ohashi, K.; Yagyu, H.; Okazaki, M.; Gotoda, T.; Nagai, R.; Kadowaki, T.; Shimano, H.; Yamada, N.; Ishibashi, S.
Hormone-sensitive lipase is involved in hepatic cholesteryl ester hydrolysis
J. Lipid Res.
49
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2008
Mus musculus
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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 (Q05469), Homo sapiens
brenda
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
brenda
Lampidonis, A.D.; Argyrokastritis, A.; Stravopodis, D.J.; Voutsinas, G.E.; Ntouroupi, T.G.; Margaritis, L.H.; Bizelis, I.; Rogdakis, E.
Cloning and functional characterization of the ovine Hormone Sensitive Lipase (HSL) full-length cDNAs: an integrated approach
Gene
416
30-43
2008
Ovis aries, Ovis aries (B3EYB8), Ovis aries (B3EYB9)
brenda
Soror, S.H.; Rao, R.; Cullum, J.
Mining the genome sequence for novel enzyme activity: characterisation of an unusual member of the hormone-sensitive lipase family of esterases from the genome of Streptomyces coelicolor A3 (2)
Protein Eng. Des. Sel.
22
333-339
2009
Streptomyces coelicolor
brenda
Langfort, J.; Jagsz, S.; Dobrzyn, P.; Brzezinska, Z.; Klapcinska, B.; Galbo, H.; Gorski, J.
Testosterone affects hormone-sensitive lipase (HSL) activity and lipid metabolism in the left ventricle
Biochem. Biophys. Res. Commun.
399
670-676
2010
Rattus norvegicus
brenda
Ogasawara, J.; Nomura, S.; Rahman, N.; Sakurai, T.; Kizaki, T.; Izawa, T.; Ishida, H.; Haga, S.; Ohno, H.
Hormone-sensitive lipase is critical mediators of acute exercise-induced regulation of lipolysis in rat adipocytes
Biochem. Biophys. Res. Commun.
400
134-139
2010
Rattus norvegicus, Rattus norvegicus Wistar
brenda
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
brenda
Shen, W.J.; Yu, Z.; Patel, S.; Jue, D.; Liu, L.F.; Kraemer, F.B.
Hormone-sensitive lipase modulates adipose metabolism through PPARgamma
Biochim. Biophys. Acta
1811
9-16
2011
Mus musculus, Mus musculus C57/BL6J
brenda
Kittilson, J.D.; Reindl, K.M.; Sheridan, M.A.
Rainbow trout (Oncorhynchus mykiss) possess two hormone-sensitive lipase-encoding mRNAs that are differentially expressed and independently regulated by nutritional state
Comp. Biochem. Physiol. A
158
52-60
2011
Oncorhynchus mykiss (E2JFF5), Oncorhynchus mykiss (E2JFF6), Oncorhynchus mykiss
brenda
Kawasaki, M.; Miura, Y.; Yagasaki, K.
Effects of sulfur amino acids, L-methionine, L-cystine and L-cysteine on lipoprotein lipase and hormone-sensitive lipase in differentiated mouse 3T3-L1 adipocytes
Cytotechnology
62
225-233
2010
Mus musculus
brenda
Pinent, M.; Prokesch, A.; Hackl, H.; Voshol, P.J.; Klatzer, A.; Walenta, E.; Panzenboeck, U.; Kenner, L.; Trajanoski, Z.; Hoefler, G.; Bogner-Strauss, J.G.
Adipose triglyceride lipase and hormone-sensitive lipase are involved in fat loss in JunB-deficient mice
Endocrinology
152
2678-2689
2011
Mus musculus
brenda
Ngo, T.D.; Ryu, B.H.; Ju, H.; Jang, E.; Park, K.; Kim, K.K.; Kim, T.D.
Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library
Acta Crystallogr. Sect. D
69
1726-1737
2013
uncultured bacterium (Q4TZQ3)
brenda
Ascione, G.; de Pascale, D.; De Santi, C.; Pedone, C.; Dathan, N.A.; Monti, S.M.
Native expression and purification of hormone-sensitive lipase from Psychrobacter sp. TA144 enhances protein stability and activity
Biochem. Biophys. Res. Commun.
420
542-546
2012
Psychrobacter sp., Psychrobacter sp. TA144
brenda
De Santi, C.; Durante, L.; Vecchio, P.D.; Tutino, M.L.; Parrilli, E.; de Pascale, D.
Thermal stabilization of psychrophilic enzymes: a case study of the cold-active hormone-sensitive lipase from Psychrobacter sp. TA144
Biotechnol. Prog.
28
946-952
2012
Psychrobacter sp., Psychrobacter sp. TA144
brenda
Wang, S.P.; Wu, J.W.; Bourdages, H.; Lefebvre, J.F.; Casavant, S.; Leavitt, B.R.; Labuda, D.; Trasler, J.; Smith, C.E.; Hermo, L.; Mitchell, G.A.
The catalytic function of hormone-sensitive lipase is essential for fertility in male mice
Endocrinology
155
3047-3053
2014
Mus musculus
brenda
Eichmann, T.O.; Kumari, M.; Haas, J.T.; Farese, R.V.; Zimmermann, R.; Lass, A.; Zechner, R.
Studies on the substrate and stereo/regioselectivity of adipose triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-acyltransferases
J. Biol. Chem.
287
41446-41457
2012
Mus musculus, Mus musculus C57BL/6
brenda
Manna, P.R.; Cohen-Tannoudji, J.; Counis, R.; Garner, C.W.; Huhtaniemi, I.; Kraemer, F.B.; Stocco, D.M.
Mechanisms of action of hormone-sensitive lipase in mouse Leydig cells: its role in the regulation of the steroidogenic acute regulatory protein
J. Biol. Chem.
288
8505-8518
2013
Mus musculus, Mus musculus MA-10
brenda
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
brenda
Marvyn, P.M.; Bradley, R.M.; Button, E.B.; Mardian, E.B.; Duncan, R.E.
Fasting upregulates adipose triglyceride lipase and hormone-sensitive lipase levels and phosphorylation in mouse kidney
Biochem. Cell Biol.
93
262-267
2015
Mus musculus
brenda
Vasilieva, E.; Dutta, S.; Malla, R.K.; Martin, B.P.; Spilling, C.D.; Dupureur, C.M.
Rat hormone sensitive lipase inhibition by cyclipostins and their analogs
Bioorg. Med. Chem.
23
944-952
2015
Rattus norvegicus
brenda
Ogiyama, T.; Yamaguchi, M.; Kurikawa, N.; Honzumi, S.; Yamamoto, Y.; Sugiyama, D.; Takakusa, H.; Inoue, S.I.
Identification of a novel hormone sensitive lipase inhibitor with a reduced potential of reactive metabolites formation
Bioorg. Med. Chem.
25
2234-2243
2017
Homo sapiens
brenda
Ogiyama, T.; Yamaguchi, M.; Kurikawa, N.; Honzumi, S.; Terayama, K.; Nagaoka, N.; Yamamoto, Y.; Kimura, T.; Sugiyama, D.; Inoue, S.I.
Design, synthesis, and pharmacological evaluation of a novel series of hormone sensitive lipase inhibitor
Bioorg. Med. Chem.
25
4817-4828
2017
Homo sapiens
brenda
Dukunde, A.; Schneider, D.; Lu, M.; Brady, S.; Daniel, R.
A novel, versatile family IV carboxylesterase exhibits high stability and activity in a broad pH spectrum
Biotechnol. Lett.
39
577-587
2017
uncultured organism (G3CRD1)
brenda
Choi, Y.H.; Lee, Y.N.; Park, Y.J.; Yoon, S.J.; Lee, H.B.
Identification of amino acids related to catalytic function of Sulfolobus solfataricus P1 carboxylesterase by site-directed mutagenesis and molecular modeling
BMB Rep.
49
349-354
2016
Saccharolobus solfataricus (A0A0E3GVY6), Saccharolobus solfataricus P1 (A0A0E3GVY6), Saccharolobus solfataricus DSM1616 (A0A0E3GVY6)
brenda
Dua, A.; Gupta, R.
Functional characterization of hormone sensitive-like lipase from Bacillus halodurans synthesis and recovery of pNP-laurate with high yields
Extremophiles
21
871-889
2017
Halalkalibacterium halodurans (Q9KAN9), Halalkalibacterium halodurans DSM 18197 (Q9KAN9)
brenda
Sun, J.; Yang, Z.; Xiao, P.; Liu, Y.; Ji, H.; Du, Z.; Chen, L.
Two isoforms of hormone-sensitive lipase b are generated by alternative exons usage and transcriptional regulation by insulin in grass carp (Ctenopharyngodon idella)
Fish Physiol. Biochem.
43
539-547
2017
Ctenopharyngodon idella
brenda
Takanashi, M.; Taira, Y.; Okazaki, S.; Takase, S.; Kimura, T.; Li, C.C.; Xu, P.F.; Noda, A.; Sakata, I.; Kumagai, H.; Ikeda, Y.; Iizuka, Y.; Yahagi, N.; Shimano, H.; Osuga, J.I.; Ishibashi, S.; Kadowaki, T.; Okazaki, H.
Role of hormone-sensitive lipase in leptin-promoted fat loss and glucose lowering
J. Artheroscler. Thromb.
24
110-1116
2017
Mus musculus (P54310)
brenda
Whytock, K.L.; Shepherd, S.O.; Wagenmakers, A.J.M.; Strauss, J.A.
Hormone-sensitive lipase preferentially redistributes to lipid droplets associated with perilipin-5 in human skeletal muscle during moderate-intensity exercise
J. Physiol.
596
2077-2090
2018
Homo sapiens (Q05469), Homo sapiens
brenda
Sommer, B.; Overy, D.P.; Haltli, B.; Kerr, R.G.
Secreted lipases from Malassezia globosa recombinant expression and determination of their substrate specificities
Microbiology
162
1069-1079
2016
Malassezia globosa (A8PUY1), Malassezia globosa (A8PUY5), Malassezia globosa (A8QCW4), Malassezia globosa (A8QDF0), Malassezia globosa, Malassezia globosa CBS 7966 (A8PUY1), Malassezia globosa CBS 7966 (A8PUY5), Malassezia globosa CBS 7966 (A8QCW4), Malassezia globosa CBS 7966 (A8QDF0), Malassezia globosa ATCC MYA-4612 (A8PUY1), Malassezia globosa ATCC MYA-4612 (A8PUY5), Malassezia globosa ATCC MYA-4612 (A8QCW4), Malassezia globosa ATCC MYA-4612 (A8QDF0)
brenda
Sanchez-Carbente, M.D.R.; Batista-Garcia, R.A.; Sanchez-Reyes, A.; Escudero-Garcia, A.; Morales-Herrera, C.; Cuervo-Soto, L.I.; French-Pacheco, L.; Fernandez-Silva, A.; Amero, C.; Castillo, E.; Folch-Mallol, J.L.
The first description of a hormone-sensitive lipase from a basidiomycete Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase
MicrobiologyOpen
6
e463
2017
Bjerkandera adusta (A0A1S5T4Z0), Bjerkandera adusta
brenda
Huang, J.; Huo, Y.; Ji, R.; Kuang, S.; Ji, C.; Xu, X.; Li, J.
Structural insights of a hormone sensitive lipase homologue Est22
Sci. Rep.
6
28550
2016
uncultured bacterium (H6BDX1)
brenda
De Koster, J.; Nelli, R.; Strieder-Barboza, C.; de Souza, J.; Lock, A.; Contreras, G.
The contribution of hormone sensitive lipase to adipose tissue lipolysis and its regulation by insulin in periparturient dairy cows
Sci. Rep.
8
13378
2018
Bos taurus (P16386)
brenda