Abstract:
:Lipoprotein lipase (LPL) catalyzes the hydrolysis of the triacylglycerol component of triacylglycerol-rich lipoproteins. There are 4 cysteine pairs that are completely conserved among LPLs of all species known. We examined the functional importance of each of the cysteine pairs in enzyme catalysis by examining LPLs produced in Cos cells by transfection. Immunoreactive LPL was produced by vectors encoding the wildtype LPL and each of the 4 cysteine-pair mutant LPLs. Enzyme activity was detectable in the wildtype enzyme, but not in 3 of the 4 Cys-->Ser mutant enzymes (C216S/C239S, C264S/C275S, and C278S/C283S). Interestingly, LPL activity was also present in the mutant (C418S/C438S), which affects the C-terminal cysteine pair, with a specific activity approximately 50% higher than that of wildtype. There is evidence that LPL contains two distinct domains consisting of the N-terminal three-quarters of the sequence connected by a flexible region to the C-terminal domain comprising the rest of the molecule. The conservation of catalytic function despite the disruption of the only disulfide bridge in the C-terminal domain of LPL indicates that the two domains can function independently of each other in enzyme catalysis.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Lo JY,Smith LC,Chan Ldoi
10.1006/bbrc.1995.1037subject
Has Abstractpub_date
1995-01-05 00:00:00pages
266-71issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(85)71037-6journal_volume
206pub_type
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