Abstract
Acyl carrier protein (ACP) is an essential component in the type II fatty acid biosynthesis (FAS II) process and is responsible for the acyl
group transfer within a series of related enzymes. In this work, theACPfrom Helicobacter pylori strain SS1 was cloned and the gene sequence
of Hpacp was deposited in the GenBank database (Accession No.: AY904356). Two forms of HpACP (apo, holo) were successfully purified
and characterized. The thermal stability of these two forms was quantitatively investigated byCDspectral analyses. The results revealed that
the holo-HpACP was more stable than apo-HpACP according to the transition midpoint temperature(Tm). Moreover, the interaction of
HpACPwith the related enzyme (b-hydroxyacyl-ACP dehydratase, HpFabZ) was determined by GST-pull down assay and surface plasmon
resonance (SPR) technique in vitro, the results showed that HpACP displays a strong binding affinity to HpFabZ (KD = 1.2 108 M). This
current work is hoped to supply useful information for better understanding the ACP features of Helicobacter pylori SS1 strain.