KEGG   ENZYME: 3.1.1.79Help
Entry
EC 3.1.1.79                 Enzyme                                 

Name
hormone-sensitive lipase;
HSL
Class
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
BRITE hierarchy
Sysname
diacylglycerol acylhydrolase
Reaction(IUBMB)
(1) diacylglycerol + H2O = monoacylglycerol + a carboxylate [RN:R05209];
(2) triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369];
(3) monoacylglycerol + H2O = glycerol + a carboxylate [RN:R07293]
Reaction(KEGG)
Substrate
diacylglycerol [CPD:C00165];
H2O [CPD:C00001];
triacylglycerol [CPD:C00422];
monoacylglycerol [CPD:C01885]
Product
monoacylglycerol [CPD:C01885];
carboxylate [CPD:C00060];
diacylglycerol [CPD:C00165];
glycerol [CPD:C00116]
Comment
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.
History
EC 3.1.1.79 created 2004
Orthology
K07188  hormone-sensitive lipase
Genes
HSA: 3991(LIPE)
PTR: 456076(LIPE)
PPS: 100975071(LIPE)
GGO: 101145804(LIPE)
PON: 100445800(LIPE)
NLE: 100603864(LIPE)
MCC: 707997(LIPE)
MCF: 102143368(LIPE)
CSAB: 103234777(LIPE)
RRO: 104658678(LIPE)
RBB: 108513895(LIPE)
CJC: 100387953(LIPE)
SBQ: 101052652(LIPE)
MMU: 16890(Lipe)
RNO: 25330(Lipe)
CGE: 100755300(Lipe)
NGI: 103744591(Lipe)
HGL: 101709284(Lipe)
CCAN: 109691865(Lipe)
OCU: 100339941(LIPE)
TUP: 102477502(LIPE)
CFA: 403607(LIPE)
AML: 100479605(LIPE)
UMR: 103680155(LIPE)
ORO: 101384261(LIPE)
FCA: 751818(LIPE)
PTG: 102952452(LIPE)
AJU: 106987707(LIPE)
BTA: 286879(LIPE)
BOM: 102266815(LIPE)
BIU: 109572731(LIPE)
PHD: 102342245(LIPE)
CHX: 100860801(LIPE)
OAS: 100169699(LIPE)
SSC: 397583(LIPE)
CFR: 102520149(LIPE)
CDK: 105090211(LIPE)
BACU: 103006716(LIPE)
LVE: 103074607(LIPE)
OOR: 101277193(LIPE)
ECB: 100069598(LIPE)
EPZ: 103558823(LIPE) 103563985
EAI: 106847929 106847941(LIPE)
MYB: 102247234(LIPE)
MYD: 102764534(LIPE)
HAI: 109374451(LIPE)
RSS: 109435701(LIPE)
PALE: 102889858(LIPE)
LAV: 100670874(LIPE)
TMU: 101361564
MDO: 103104890(LIPE)
SHR: 100926393(LIPE)
AAM: 106487870(LIPE)
ASN: 102386893(LIPE)
AMJ: 102571969(LIPE)
CPIC: 101953217(LIPE)
ACS: 107982284
PVT: 110086763(LIPE)
PBI: 103054092(LIPE)
GJA: 107106853(LIPE) 107117837
XLA: 100174796(lipe.L) 108697769(lipe.S)
XTR: 733899(lipe)
NPR: 108799329(LIPE)
DRE: 557893(lipeb)
IPU: 108256376(lipe) 108272659
AMEX: 103030794(lipe) 103036112
LCO: 104927333(lipe) 104928056
MZE: 101473301 101485272(lipe)
OLA: 101157970(lipe) 101160745
XMA: 102217205 102234893(lipe)
PRET: 103473021 103477914(lipe)
NFU: 107379673(lipe) 107394884
CSEM: 103388799(lipe) 103393953
LCF: 108880754(lipe) 108899366
HCQ: 109513537 109531659(lipe)
BPEC: 110168856 110174235(lipe)
SFM: 108922191
LCM: 102346636(LIPE)
CIN: 100181083
SPU: 585712
APLC: 110988815
SKO: 100376662
DME: Dmel_CG11055(Hsl)
DSI: Dsimw501_GD11499(Dsim_GD11499)
MDE: 101899540
AAG: 5566934
AME: 413702
BIM: 100748813
BTER: 100646474
SOC: 105198580
AEC: 105143573
ACEP: 105620501
PBAR: 105428403
HST: 105188918
LHU: 105676433
PGC: 109856830
NVI: 100120573
TCA: 664547
DPA: 109543096
NVL: 108569775
BMOR: 101737209
PRAP: 110998313
PXY: 105392962
API: 100159927
DNX: 107171212
ZNE: 110826823
FCD: 110844206
CEL: CELE_C46C11.1(hosl-1)
CBR: CBG14512
TSP: Tsp_02264
CRG: 105345018
MYI: 110445915
OBI: 106878881
SHX: MS3_01741
EPA: 110241065
HMG: 100210426
AQU: 105314138
SPAR: SPRG_01501
 » show all
Taxonomy
Reference
1  [PMID:10940339]
  Authors
Holm C, Osterlund T, Laurell H, Contreras JA.
  Title
Molecular mechanisms regulating hormone-sensitive lipase and lipolysis.
  Journal
Annu Rev Nutr 20:365-93 (2000)
DOI:10.1146/annurev.nutr.20.1.365
Reference
2  [PMID:7240206]
  Authors
Fredrikson G, Stralfors P, Nilsson NO, Belfrage P.
  Title
Hormone-sensitive lipase of rat adipose tissue. Purification and some properties.
  Journal
J Biol Chem 256:6311-20 (1981)
Reference
3  [PMID:14169138]
  Authors
VAUGHAN M, BERGER JE, STEINBERG D.
  Title
HORMONE-SENSITIVE LIPASE AND MONOGLYCERIDE LIPASE  ACTIVITIES IN ADIPOSE TISSUE.
  Journal
J Biol Chem 239:401-9 (1964)
Reference
4  [PMID:8912675]
  Authors
Osterlund T, Danielsson B, Degerman E, Contreras JA, Edgren G, Davis RC, Schotz MC, Holm C.
  Title
Domain-structure analysis of recombinant rat hormone-sensitive lipase.
  Journal
Biochem J 319 ( Pt 2):411-20 (1996)
Reference
5  [PMID:3196730]
  Authors
Lee FT, Adams JB, Garton AJ, Yeaman SJ.
  Title
Hormone-sensitive lipase is involved in the hydrolysis of lipoidal derivatives of estrogens and other steroid hormones.
  Journal
Biochim Biophys Acta 963:258-64 (1988)
DOI:10.1016/0005-2760(88)90289-5
Reference
6  [PMID:9162045]
  Authors
Wei S, Lai K, Patel S, Piantedosi R, Shen H, Colantuoni V, Kraemer FB, Blaner WS.
  Title
Retinyl ester hydrolysis and retinol efflux from BFC-1beta adipocytes.
  Journal
J Biol Chem 272:14159-65 (1997)
DOI:10.1074/jbc.272.22.14159
Reference
7  [PMID:2794798]
  Authors
Tsujita T, Ninomiya H, Okuda H.
  Title
p-nitrophenyl butyrate hydrolyzing activity of hormone-sensitive lipase from bovine adipose tissue.
  Journal
J Lipid Res 30:997-1004 (1989)
Reference
8  [PMID:14725507]
  Authors
Yeaman SJ.
  Title
Hormone-sensitive lipase--new roles for an old enzyme.
  Journal
Biochem J 379:11-22 (2004)
DOI:10.1042/BJ20031811
Other DBs
ExplorEnz - The Enzyme Database: 3.1.1.79
IUBMB Enzyme Nomenclature: 3.1.1.79
ExPASy - ENZYME nomenclature database: 3.1.1.79
BRENDA, the Enzyme Database: 3.1.1.79

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