Substrate preferences of a lysophosphatidylcholine acyltransferase highlight its role in phospholipid remodeling.

Abstract:

:An important enzyme involved in phospholipid turnover is the acyl-CoA: lysophosphatidylcholine acyltransferase (LPCAT). Here, we report characterization of a newly discovered human LPCAT (LPCAT3), which has distinct substrate preferences strikingly consistent with a role in phosphatidylcholine (PtdCho) remodeling and modulating fatty acid composition of PtdCho. LPCAT3 prefers lysophosphatidylcholine (lysoPtdCho) with saturated fatty acid at the sn-1 position and exhibits acyl donor preference towards linoleoyl-CoA and arachidonoyl-CoA. Furthermore, LPCAT3 is active in mediating 1-O-alkyl-sn-glycero-3-phosphocholine acylation with long chain fatty acyl-CoAs to generate 1-O-alkyl-phosphatidylcholine, another very important constitute of mammalian membrane systems. These properties are precisely the known attributes of LPCAT previously ascribed to the isoform involved in Lands' cycle, and thus strongly suggest that LPCAT3 is involved in phospholipids remodeling to achieve appropriate membrane lipid fatty acid composition.

journal_name

Lipids

journal_title

Lipids

authors

Kazachkov M,Chen Q,Wang L,Zou J

doi

10.1007/s11745-008-3233-y

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

895-902

issue

10

eissn

0024-4201

issn

1558-9307

journal_volume

43

pub_type

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