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Information on EC 3.1.1.79 - hormone-sensitive lipase

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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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UNIPROT: Q0GMU2
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Word Map
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, este5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hormone-sensitive lipase
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HSL
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-
-
-
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl acetate + H2O
?
show the reaction diagram
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%)
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-
?
p-nitrophenyl butyrate + H2O
?
show the reaction diagram
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 caproate + H2O
?
show the reaction diagram
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%)
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-
?
p-nitrophenyl caprylate + H2O
?
show the reaction diagram
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%)
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-
?
p-nitrophenyl decanoate + H2O
?
show the reaction diagram
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%)
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-
?
p-nitrophenyl palmitate + H2O
?
show the reaction diagram
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 stearate + H2O
?
show the reaction diagram
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%)
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.06
p-nitrophenyl butyrate
Vmax value is 493.6 microM/min
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q0GMU2_9BACT
297
0
31916
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
purified enzyme is broadly stable within a pH range of 5.5-9.0
690779
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Biochem. Biophys. Res. Commun.
379
553-556
2009
uncultured bacterium (Q0GMU2)
Manually annotated by BRENDA team