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.
中科院分区:
文献类型:
--
作者:
Chen, Aochiu;Jiang, Ziran;Burkart, Michael D.
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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影响因子:
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通讯作者:
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10.1073/pnas.1702849114
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Burkart, Michael D.
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