KEGG   ENZYME: 3.1.1.34
Entry
EC 3.1.1.34                 Enzyme                                 

Name
lipoprotein lipase;
clearing factor lipase;
diacylglycerol lipase;
postheparin esterase;
diglyceride lipase;
postheparin lipase;
diacylglycerol hydrolase;
lipemia-clearing factor;
hepatic triacylglycerol lipase;
LIPC (gene name);
LPL (gene name);
triacylglycero-protein acylhydrolase
Class
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
Sysname
triacylglycerol acylhydrolase (lipoprotein-dependent)
Reaction(IUBMB)
triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Reaction(KEGG)
R01369;
(other) R01350
Substrate
triacylglycerol [CPD:C00422];
H2O [CPD:C00001]
Product
diacylglycerol [CPD:C00165];
carboxylate [CPD:C00060]
Comment
Hydrolyses triacylglycerols and diacylglycerol in chylomicrons and low-density lipoprotein particles. Human protein purified from post-heparin plasma (LPL) shows no activity against triglyceride in the absence of added lipoprotein. The principal reaction sequence of that enzyme is triglyceride -> 1,2-diglyceride -> 2-monoglyceride. The hepatic enzyme (LIPC) also hydrolyses triglycerides and phospholipids present in circulating plasma lipoproteins.
History
EC 3.1.1.34 created 1972, modified 1976
Pathway
ec00561  Glycerolipid metabolism
Orthology
K01059  lipoprotein lipase
Genes
HSA: 4023(LPL)
PTR: 464031(LPL)
PPS: 100986925(LPL)
GGO: 101124245(LPL)
PON: 100443394(LPL)
NLE: 100584438(LPL)
MCC: 712887(LPL)
MCF: 102129758(LPL)
CSAB: 103215415(LPL)
RRO: 104662456(LPL)
RBB: 108526485(LPL)
CJC: 100409187(LPL)
SBQ: 101050033(LPL)
MMU: 16956(Lpl)
MCAL: 110299545(Lpl)
MPAH: 110336613(Lpl)
RNO: 24539(Lpl)
MUN: 110541256(Lpl)
CGE: 100689191(Lpl)
NGI: 103747648(Lpl)
HGL: 101703016(Lpl)
CCAN: 109695324(Lpl)
OCU: 100340171(LPL)
TUP: 102492328(LPL)
CFA: 403626(LPL)
VVP: 112925544(LPL)
AML: 100482804(LPL)
UMR: 103676703(LPL)
UAH: 113270022(LPL)
ORO: 101380450(LPL)
ELK: 111154450
FCA: 727696(LPL)
PTG: 102967736(LPL)
PPAD: 109261142(LPL)
AJU: 106971857(LPL)
BTA: 280843(LPL)
BOM: 102266770(LPL)
BIU: 109563092(LPL)
BBUB: 102412415(LPL)
CHX: 100860750(LPL)
OAS: 443408(LPL)
SSC: 397537(LPL)
CFR: 102520179(LPL)
CDK: 105094532(LPL)
BACU: 103005101
LVE: 103083746(LPL)
OOR: 101284828(LPL)
DLE: 111169014(LPL)
PCAD: 102976943(LPL)
ECB: 100055358(LPL)
EPZ: 103559571(LPL)
EAI: 106831205(LPL)
MYB: 102247387(LPL)
MYD: 102759852(LPL)
MNA: 107535437(LPL)
HAI: 109382488(LPL)
DRO: 112305220(LPL)
PALE: 102892638(LPL)
RAY: 107503749(LPL)
MJV: 108384237(LPL)
LAV: 100667686(LPL)
TMU: 101345905
MDO: 100033067(LPL)
SHR: 100933361(LPL)
PCW: 110196400(LPL)
OAA: 100077350(LPL)
GGA: 396219(LPL)
MGP: 100544844(LPL)
CJO: 107306443(LPL)
NMEL: 110389877(LPL)
APLA: 101796218(LPL)
ACYG: 106040417(LPL)
TGU: 100223817(LPL)
LSR: 110472801(LPL)
SCAN: 103821279(LPL)
GFR: 102041807(LPL)
FAB: 101814126(LPL)
PHI: 102111905(LPL)
PMAJ: 107216453(LPL)
CCAE: 111941733(LPL)
CCW: 104689737(LPL)
ETL: 114063704(LPL)
FPG: 101913413(LPL)
FCH: 102046454(LPL)
CLV: 102097018(LPL)
EGZ: 104123360(LPL)
NNI: 104011947(LPL)
ACUN: 113490034(LPL)
PADL: 103925585(LPL)
ASN: 102368909(LPL)
AMJ: 102573889(LPL)
PSS: 102456906(LPL)
CMY: 102941095
CPIC: 101932991(LPL)
ACS: 100556298(lpl)
PVT: 110083190(LPL)
PBI: 103057093(LPL)
PMUR: 107286300(LPL)
TSR: 106547738(LPL)
PMUA: 114587743(LPL)
GJA: 107118995(LPL)
XLA: 108706825(lpl.S) 108712233(lpl.L)
XTR: 100127862(lpl)
NPR: 108804916(LPL)
IPU: 108271131(LPL) 108280930
TRU: 101062428(lpl) 101068642
ONL: 100534504(lpl) 100689908
OLA: 101160309(lpl) 101160547
XCO: 114150801 114151199(lpl)
PRET: 103463532 103463534(lpl)
NFU: 107393172 107393174(lpl)
KMR: 108230795(lpl) 108230848
ALIM: 106521565(lpl) 106521567
CSEM: 103397050 103397060(lpl)
POV: 109625830(lpl) 109625897
LCF: 108881396 108881397(lpl)
SDU: 111232066(lpl) 111232091
SLAL: 111654280(lpl) 111654288
BPEC: 110160148
MALB: 109967464
SFM: 108919920 108919924(lpl)
LCM: 102349247(LPL) 102362907
CMK: 103183498(lpl) 103183499
RTP: 109922304(lpl) 109922306
DSR: 110191785
LCQ: 111690990
AAG: 5567092
PMAC: 106717696
HAW: 110383800
 » show all
Reference
1  [PMID:4703566]
  Authors
Egelrud T, Olivecrona T.
  Title
Purified bovine milk (lipoprotein) lipase: activity against lipid substrates in the absence of exogenous serum factors.
  Journal
Biochim Biophys Acta 306:115-27 (1973)
DOI:10.1016/0005-2760(73)90215-4
Reference
2  [PMID:5441398]
  Authors
Fielding CJ.
  Title
Human lipoprotein lipase. I. Purification and substrate specificity.
  Journal
Biochim Biophys Acta 206:109-17 (1970)
DOI:10.1016/0005-2744(70)90087-2
Reference
3  [PMID:5466051]
  Authors
Greten H, Levy RI, Fales H, Fredrickson DS.
  Title
Hydrolysis of diglyceride and glyceryl monoester diethers with "lipoprotein lipase".
  Journal
Biochim Biophys Acta 210:39-45 (1970)
DOI:10.1016/0005-2760(70)90059-7
Reference
4  [PMID:5076762]
  Authors
Morley N, Kuksis A.
  Title
Positional specificity of lipoprotein lipase.
  Journal
J Biol Chem 247:6389-93 (1972)
Reference
5  [PMID:5168777]
  Authors
Nilsson-Ehle P, Belfrage P, Borgstrom B.
  Title
Purified human lipoprotein lipase: positional specificity.
  Journal
Biochim Biophys Acta 248:114-20 (1971)
DOI:10.1016/0005-2760(71)90081-6
Reference
6  [PMID:15284087]
  Authors
Santamarina-Fojo S, Gonzalez-Navarro H, Freeman L, Wagner E, Nong Z
  Title
Hepatic lipase, lipoprotein metabolism, and atherogenesis.
  Journal
Arterioscler Thromb Vasc Biol 24:1750-4 (2004)
DOI:10.1161/01.ATV.0000140818.00570.2d
Other DBs
ExplorEnz - The Enzyme Database: 3.1.1.34
IUBMB Enzyme Nomenclature: 3.1.1.34
ExPASy - ENZYME nomenclature database: 3.1.1.34
BRENDA, the Enzyme Database: 3.1.1.34
CAS: 9004-02-8

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