Literature summary for 3.1.1.34 extracted from

Murano, T.; Sako, T.; Oikawa, S.; Shirai, K.
The recovery of dysfunctional lipoprotein lipase (Asp204-Glu) activity by modification of substrate (2005), Atherosclerosis, 183, 101-107.

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Protein Variants

Protein Variants	Comment	Organism
D204E	homozygous missense mutation identified in a patient with severe hypertriglyceridemia, post-heparin enzyme mass is almost normal, but the enzyme activity is remarkably decreased. In presence of phosphatidylethenolamine, phospatidylserine, and cardiolipin as emulsifier, triolein-hydrolizing activity of the mutant is higher than wild-type activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	functional deficiency of enzyme in a patient with severe hypertriglyceridemia	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	patient with severe hypertriglyceridemia, post-heparin enzyme mass is almost normal, but the enzyme activity is remarkably decreased	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
triolein + H2O	mutant D204 E, very low activity in presence of emulsifier Triton X-100 or phosphatidylcholine. In presence of phosphatidylethenolamine, phospatidylserine, and cardiolipin as emulsifier, triolein-hydrolizing activity of the mutant is higher than wild-type activity	Homo sapiens	dioleylglycerol + oleate	-	?

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Release 2023.1 (January 2023)