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Information on EC 3.1.1.79 - hormone-sensitive lipase and Organism(s) Bos taurus and UniProt Accession P16386

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EC Tree
     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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Bos taurus
UNIPROT: P16386
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hormone-sensitive lipase, alpha/beta hydrolase, hsl protein, secreted lipase, est22, est25, mgmdl2, cardiac hsl, est06, rv3097c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hormone-sensitive lipase
-
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
2-oleylglycerol + oleate
show the reaction diagram
-
-
-
-
?
cholesteryl oleate + H2O
cholesterol + oleate
show the reaction diagram
dehydroepiandrosterone oleate + H2O
dehydroepiandrosterone + oleate
show the reaction diagram
-
12.9% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
diacylglycerol + H2O
monoacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
estradiol-17-beta-oleate + H2O
17-beta-estradiol + oleate
show the reaction diagram
-
17.9% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
estradiol-17-beta-palmitate + H2O
17-beta-estradiol + palmitate
show the reaction diagram
-
18.3% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
monoacylglycerol + H2O
glycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl laurate + H2O
p-nitrophenol + laurate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
show the reaction diagram
-
-
-
-
?
testosterone oleate + H2O
testosterone + oleate
show the reaction diagram
-
1.4% of activity with 1-oleoyl-2-oleylglycerol
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
triolein + H2O
dioleoylglycerol + oleate
show the reaction diagram
-
-
-
-
?
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
diacylglycerol + H2O
monoacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
monoacylglycerol + H2O
glycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
diisopropyl fluorophosphate
-
complete inhibition
diisopropylfluorophosphate
Emulgen 120
-
0.1%, 955 of cholesteryl oleate hydrolysis
Hg2+
-
0.005 mM, approx. 50% inhibition, 0.02 mM, approx. 70% inhibition
NaF
-
20 mM, 50% inhibition of p-nitrophenyl butyrate hydrolysis, 70% of triolein hydrolysis, 60% of cholesteryl hydrolysis
phenylmethanesulfonyl fluoride
-
0.01 mM, approx. 75% inhibition, 0.01 mM, approx. 90% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyclic AMP-dependent protein kinase
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phosphorylation, 40% activation of triolein hydrolyzing activity
-
HSL inhibitor
-
reduced activity in macrophage foam cells due to increased activity of an inhibitor protein
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phosphatidylcholine
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0.075 mM, slight activation upon incorporation into cholestryl oleate liquid crystals
phosphatidylethanolamine
-
0.075 mM, approx. 6fold activation upon incorporation into cholestryl oleate liquid crystals
Phospholipid
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.099
cholesteryl oleate
0.164
p-nitrophenyl butyrate
-
37°C, pH 6.8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.068
-
cholesteryl oleate hydroylsis
0.3
-
hydrolysis of estradiol-17-beta-oleate
0.8
-
hydrolysis of p-nitrophenyl laurate
0.9
-
hydrolysis of p-nitrophenyl palmitate
1.45
-
hydrolysis of cholesteryl oleate
2.6
-
hydrolysis of 1-oleoyl-2-oleylglycerol
2.8
-
1-oleoyl-2-oleylglycerol
22
-
hydrolysis of p-nitrophenyl butyrate
3.8
-
hydrolysis of cholesteryl oleate
30
-
hydrolysis of 1-oleoyl-2-O-oleylglycerol
4.7
-
hydrolysis of p-nitrophenyl acetate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
approx. 50% of maximal activity at pH 5.5 and pH 8.5, respectively
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cotyledon
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIPS_BOVIN
756
0
82641
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 500 mM phosphate buffer, pH 7.0, 50% glycerol, 100 mM benzamidine, 1 mM dithiothreitol, 0.2% C13E12, 5 mg/ml leupeptin and 1 mg/ml pepstatin, at least 2 months, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH 5.0, DE-52, hydroxyapatite
-
pH 5.0, DE-52, hydroxyapatite, Phenyl-Sepharose, Heparin-Sepharose
-
pH 5.0, DE-52, hydroxylapatite, Phenyl-Sepharose, heparin-Sepharose
-
pH 5.0, DE-52, Phenyl-Sepharose, Mono Q, Mono S
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsujita,T.; Okuda, H.
Hydrolysis of cholesteryl oleate liquid crystals by hormon-sensitive lipase
J. Biochem.
113
264-269
1993
Bos taurus
Manually annotated by BRENDA team
Lee, F.T.; Adams, J.B.; Garton, A.J.; Yeaman, S.J.
Hormone-sensitive lipase is involved in the hydrolysis of lipoidal derivatives of estrogens and other steroid hormones
Biochim. Biophys. Acta
963
258-264
1988
Bos taurus
Manually annotated by BRENDA team
Tsujita, T.; Ninomiya, H.; Okuda, H.
p-Nitrophenyl butyrate hydrolyzing activity of hormone-sensitive lipase from bovine adipose tissue
J. Lipid Res.
30
997-1004
1989
Bos taurus
Manually annotated by BRENDA team
Yeaman, S.J.; Smith, G.M.; Jepson, C.A.; Wood, S.L.; Emmison, N.
The multifunctional role of hormone-sensitive lipase in lipid metabolism
Adv. Enzyme Regul.
34
355-370
1994
Bos taurus
Manually annotated by BRENDA team
Small, C.A.; Garton, A.J.; Yeaman, S.J.
The presence and role of hormone-sensitive lipase in heart muscle
Biochem. J.
258
67-72
1989
Bos taurus
Manually annotated by BRENDA team
Cordle, S.R.; Colbran, R.J.; Yeaman, S.J.
Hormone-sensitive lipase from bovine adipose tissue
Biochim. Biophys. Acta
887
51-57
1986
Bos taurus
Manually annotated by BRENDA team
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
Biochem. Biophys. Res. Commun.
376
36-39
2008
Bos taurus (P16386), Bos taurus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team