The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins
The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins
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辅酶 A 衍生物和酰基载体蛋白磷酸泛酰基转移酶 SchPPT 的底物混杂
DOI：
10.1007/s00203-015-1179-z
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发表时间：
2016-03-01
影响因子：
2.8
通讯作者：
Li，Yong-Quan
中科院分区：
文献类型：
--
作者：
Wang，Yue-Yue;Luo，Hong-Dou;Li，Yong-Quan
磷酸泛酰巯基乙胺基转移酶（PPTases）催化所有生物体中脂肪酸脱氢酶（FAS）中酰基载体蛋白（ACP）、聚酮脱氢酶中ACP和非核糖体肽合成酶（NRPS）中肽基载体蛋白（PCP）的翻译后修饰。一些细菌PPT酶对ACP/PCP和/或辅酶A（CoA）/CoA类似物具有广泛的底物特异性，分别促进它们在宿主中的代谢物产生和/或ACP/PCP的标记中的应用。在此，来自Streptomyces chattanoogensis L10的II组PPT酶SchPPT被表征为接受异源ACP和乙酰辅酶A。因此，SchPPT是一种混杂的PPT酶，可用于异源细菌宿主中聚酮化合物的生产和ACP的标记。
Phosphopantetheinyl transferases (PPTases) catalyze the posttranslational modification of acyl carrier proteins (ACPs) in fatty acid synthases (FASs), ACPs in polyketide synthases, and peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs) in all organisms. Some bacterial PPTases have broad substrate specificities for ACPs/PCPs and/or coenzyme A (CoA)/CoA analogs, facilitating their application in metabolite production in hosts and/or labeling of ACPs/PCPs, respectively. Here, a group II PPTase SchPPT fromStreptomyces chattanoogensisL10 was characterized to accept a heterologous ACP and acetyl-CoA. Thus, SchPPT is a promiscuous PPTase and may be used on polyketide production in heterologous bacterial host and labeling of ACPs.