Literature summary for 3.1.1.34 extracted from

Bensadoun, A.; Ehnholm, C.; Steinberg, D.; Brown, W.V.
Purification and characterization of lipoprotein lipase from pig adipose tissue (1974), J. Biol. Chem., 249, 2220-2227.

Search for more literature for 3.1.1.34

Activating Compound

Activating Compound	Comment	Organism	Structure
apolipoprotein-Glu	activates	Sus scrofa
heparin	weak stimulation	Sus scrofa

General Stability

General Stability	Organism
the partially purified enzyme at later stages is stabilized by the inclusion of 20% glycerol in the buffer	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
apolipoprotein-Ala	-	Sus scrofa
apolipoprotein-Ser	-	Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
60000	-	1 * 60000, SDS-PAGE	Sus scrofa
62000	-	gel filtration	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
adipose tissue	-	Sus scrofa	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
56.95	-	-	Sus scrofa

Storage Stability

Storage Stability	Organism
-70°C, 1 mg bovine serum albumin per ml or 50% glycerol, stable for several days	Sus scrofa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
triolein + H2O	-	Sus scrofa	?	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 60000, SDS-PAGE	Sus scrofa

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.8	-	hydrolysis of triolein	Sus scrofa

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Release 2023.1 (January 2023)