Abstract:
:Lecithin-cholesterol acyltransferase (LCAT) is responsible for the formation of cholesterol esters in plasma and is implicated in the removal of excess cholesterol from peripheral tissues. It is generally accepted that the catalytic mechanism of LCAT is similar to that of serine proteases and lipases involving a Ser, a His, and an acidic amino acid residue. Ser181 in LCAT has been previously identified as a catalytic residue; however, the active site His and acidic residue have not yet been identified. In this study we have used a variety of approaches to identify the putative active site histidine. Alignments of LCAT sequences across various species indicate that the four histidines at positions 180, 263, 368, and 377 are conserved and could be involved in catalysis. Based on the observation that the members of the triad preserve the same orientation in the primary sequence of a large number of lipases, we eliminated His180 as a potential candidate. Mutational analysis along with functional assays show that, in contrast to the replacement of His263 and His368, the replacement of the His at position 377 with Gly, Ala, or Ser obliterates LCAT activity with interfacial and water-soluble substrates, thus indicating a role of His377 in catalysis.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Adimoolam S,Lee YP,Jonas Adoi
10.1006/bbrc.1997.7995subject
Has Abstractpub_date
1998-02-13 00:00:00pages
337-41issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(97)97995-Xjournal_volume
243pub_type
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