Lipopolysaccharide biosynthesis without the lipids: recognition promiscuity of Escherichia coli heptosyltransferase I.

Lipopolysaccharide biosynthesis without the lipids: recognition promiscuity of Escherichia coli heptosyltransferase I.
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DOI:
10.1021/bi201581b
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发表时间:
2011-12-13
期刊:
影响因子:
2.9
通讯作者:
Taylor, Erika A.
Taylor, Erika A.
中科院分区:
生物学3区
文献类型:
--
作者:
Czyzyk, Daniel J.;Liu, Cassie;Taylor, Erika A.

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庚糖基转移酶I(HepI)负责将L-甘油-D-甘露庚糖转移到脂多糖(LPS)生长核心区的3-脱氧-α-D-辛-2-吡喃葡萄糖酸(Kdo)。HepI与大肠杆菌HepI LipidA完全脱酰类似物的催化效率是完全酰化底物的12倍,kcat/Km为2.7 × 106 M−1 s−1,而Kdo 2-LipidA底物的kcat/Km为2.2 × 105 M−1 s−1。这不仅是首次证明LPS生物合成酶通过不存在脂质而被催化增强,而且这一结果对现在被认为利用脱酰化底物的下游酶具有重要意义。
Heptosyltransferase I (HepI) is responsible for the transfer of L-glycero-D-manno-heptose to a 3-deoxy-α-D-oct-2-ulopyranosonic acid (Kdo) of the growing core region of lipopolysaccharide (LPS). The catalytic efficiency of HepI with the fully deacylated analogue of Escherichia coli HepI LipidA is 12-fold greater than with the fully acylated substrate, with a kcat/Km of 2.7 × 106 M−1 s−1, compared to a value of 2.2 × 105 M−1 s−1 for the Kdo2-LipidA substrate. Not only is this is the first demonstration that an LPS biosynthetic enzyme is catalytically enhanced by the absence of lipids, this result has significant implications for downstream enzymes that are now thought to utilize deacylated substrates.
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