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Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism.

Abstract：

:Very-long-chain acyl-CoA synthetases (VLCS) activate very-long-chain fatty acids (VLCFA) containing 22 or more carbons to their CoA derivatives. We cloned the human ortholog (hVLCS) of the gene encoding the rat liver enzyme (rVLCS). Both hVLCS and rVLCS contain 620 amino acids, are expressed primarily in liver and kidney, and have a potential peroxisome targeting signal 1 (-LKL) at their carboxy termini. When expressed in COS-1 cells, hVLCS activated the VLCFA lignoceric acid (C24:0), a long-chain fatty acid (C16:0), and two branched-chain fatty acids, phytanic acid and pristanic acid. Immunofluorescence and immunoblot studies localized hVLCS to both peroxisomes and endoplasmic reticulum. In peroxisomes of HepG2 cells, hVLCS was topographically oriented facing the matrix and not the cytoplasm. This orientation, coupled with the observation that hVLCS activates branched-chain fatty acids, suggests that hVLCS could play a role in the intraperoxisomal reactivation of pristanic acid produced via alpha-oxidation of phytanic acid.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Steinberg SJ,Wang SJ,Kim DG,Mihalik SJ,Watkins PA

doi

10.1006/bbrc.1999.0510

subject

Has Abstract

pub_date

1999-04-13 00:00:00

pages

615-21

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)90510-7

journal_volume

257

pub_type

杂志文章

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