Enzymatic characterization of a human acyltransferase activity.

ABSTRACT:

Background

Non-histone protein acylation is increasingly recognized as an important posttranslational modification, but little is known as to the biochemical properties of protein serine acylating enzymes.

Methodology/principal findings

We here report that we have identified a metal-stimulated serine octanoyltransferase activity in microsomes from human erythroleukemic (HEL) cells. The HEL acylating enzyme was linear with respect to time and protein, exhibited a neutral pH optimum (stimulated by cobalt and zinc), and inhibited by chelating reagents. Hydroxylamine treatment removed most, but not all, of the attached radioactivity. A salt extract of microsomal membranes contained the major portion of enzyme activity, indicating that this acyltransferase is not an integral memb

SUBMITTER: Ozawa A 

PROVIDER: S-EPMC2672172 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature