Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel-Reference-Cited by-同舟云学术

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Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel

Published:2001-12-18 Issue:26 Volume:98 Page:14808-14813
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Tsai S.-C.,Miercke L. J. W.,Krucinski J.,Gokhale R.,Chen J. C.- H.,Foster P. G.,Cane D. E.,Khosla C.,Stroud R. M.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference28 articles.

1. Harnessing the Biosynthetic Code: Combinations, Permutations, and Mutations

2. Modular organization of genes required for complex polyketide biosynthesis

3. Repositioning of a Domain in a Modular Polyketide Synthase to Promote Specific Chain Cleavage

4. Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel "unnatural" natural products

5. Manipulation of macrolide ring size by directed mutagenesis of a modular polyketide synthase

Cited by 195 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structural basis for intermodular communication in assembly-line polyketide biosynthesis;Nature Chemical Biology;2024-08-23

2. Substrate Trapping in Polyketide Synthase Thioesterase Domains: Structural Basis for Macrolactone Formation;ACS Catalysis;2024-08-06

3. Structure and Mechanisms of Assembly-Line Polyketide Synthases;Annual Review of Biochemistry;2024-08-02

4. Substrate Trapping in Polyketide Synthase Thioesterase Domains: Structural Basis for Macrolactone Formation;2024-06-20

5. Structural Basis for Intermodular Communication in Assembly-Line Polyketide Biosynthesis;2024-05-05

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