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Premutilin Synthase: Ring Rearrangement by a Class II Diterpene Cyclase.

ABSTRACT: Biosynthesis of the complex diterpenoid antibiotic pleuromutilin relies on a bifunctional (di)terpene synthase, and here site-directed mutagenesis was used to knockout either of the two active sites. This enabled characterization of the novel ring contracted intermediate produced by the initiating class II diterpene cyclase active site. Quantum chemical calculations further indicate the importance of reactant configuration for this intriguing ring rearrangement.

SUBMITTER: Xu M

PROVIDER: S-EPMC5848098 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Premutilin Synthase: Ring Rearrangement by a Class II Diterpene Cyclase.

Xu Meimei M Jia Meirong M Hong Young J YJ Yin Xihou X Tantillo Dean J DJ Proteau Philip J PJ Peters Reuben J RJ

Organic letters 20180201 4

Biosynthesis of the complex diterpenoid antibiotic pleuromutilin relies on a bifunctional (di)terpene synthase, and here site-directed mutagenesis was used to knockout either of the two active sites. This enabled characterization of the novel ring contracted intermediate produced by the initiating class II diterpene cyclase active site. Quantum chemical calculations further indicate the importance of reactant configuration for this intriguing ring rearrangement. ...[more]

PMID: 29388775

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Magnesium-specific ring expansion/contraction catalysed by the class II diterpene cyclase from pleuromutilin biosynthesis.

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Characterization and inhibition of a class II diterpene cyclase from Mycobacterium tuberculosis: implications for tuberculosis.

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