Enzymology of standalone elongating ketosynthases.

Enzymology of standalone elongating ketosynthases.
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DOI:
10.1039/d1sc07256k
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发表时间:
2022-04-13
期刊:
影响因子:
8.4
通讯作者:
Burkart, Michael D.
Burkart, Michael D.
中科院分区:
化学1区
文献类型:
--
作者:
Chen, Aochiu;Jiang, Ziran;Burkart, Michael D.

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β-酮脂酰-酰基载体蛋白合酶或酮合酶(KS)通过脱羧Claisen样缩合催化脂肪酸和聚酮化合物生物合成中的碳-碳键形成。在原核生物中,独立的延伸KS与酰基载体蛋白(ACP)相互作用,其在延伸循环中将底物穿梭于每个伴侣酶以进行催化。尽管自KS在E.随着KSs在大肠杆菌中的研究进展,KSs复杂的作用机制仍在不断被揭示,包括门控基序、KS-ACP相互作用、底物识别和传递以及在不饱和脂肪酸生物合成中的作用。在这篇综述中,我们总结了最新的研究,主要是通过结构生物学和分子探针的设计,揭示了新兴的独立延伸KS酶学。酮基化酶(KSs)接受来自酰基载体蛋白(ACP)的底物以催化脂肪酸和聚酮化合物生物合成中的碳-碳键形成。在这篇综述中,我们描述了独立的延伸酮酶的酶学,重点是酶门。
The β-ketoacyl-acyl carrier protein synthase, or ketosynthase (KS), catalyses carbon–carbon bond formation in fatty acid and polyketide biosynthesis via a decarboxylative Claisen-like condensation. In prokaryotes, standalone elongating KSs interact with the acyl carrier protein (ACP) which shuttles substrates to each partner enzyme in the elongation cycle for catalysis. Despite ongoing research for more than 50 years since KS was first identified in E. coli, the complex mechanism of KSs continues to be unravelled, including recent understanding of gating motifs, KS–ACP interactions, substrate recognition and delivery, and roles in unsaturated fatty acid biosynthesis. In this review, we summarize the latest studies, primarily conducted through structural biology and molecular probe design, that shed light on the emerging enzymology of standalone elongating KSs. Ketosynthases (KSs) accept substrates from the acyl carrier protein (ACP) to catalyse carbon–carbon bond formation in fatty acid and polyketide biosynthesis. In this review, we delineate the enzymology of standalone elongating ketosynthases with a focus on the enzyme gates.
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