MR Pelvimetry

Schäffer, Leonhard; Beinder, Ernst; Ra, Kubik-Huch

doi:10.1007/174_2017_2

Cited by 1 publication

(3 citation statements)

References 28 publications

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“…17 A recent report from the Wencewicz group reported a cysteine nucleophile in a TE domain is required for cyclization of the β-lactone product obafluorin. 18 It was proposed that the thioester intermediate is at a higher ground state energy compared to the oxyester, and thus is favorable in driving β-lactone formation. 18…”

Section: Resultsmentioning

confidence: 99%

“…18 It was proposed that the thioester intermediate is at a higher ground state energy compared to the oxyester, and thus is favorable in driving β-lactone formation. 18…”

Section: Resultsmentioning

confidence: 99%

“…Instead, the product appears to be prone to hydrolysis, analogous to the cysteine to serine mutation observed in obafluorin TE domain. 18 Although it is not clear whether such hydrolysis occurs as a S2040-sorbyl oxyster, or direct hydrolysis from the ACP, this result confirms the necessity of the cysteine as an active site nucleophile.…”

Section: Ku42 Hrpks-te Substrate Scope and Proposed Reaction Mechanismmentioning

confidence: 93%

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Thioesterase-Catalyzed Aminoacylation and Thiolation of Polyketides in Fungi

et al. 2019

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Fungal highly reducing polyketide synthases (HRPKSs) biosynthesize polyketides using a single set of domains iteratively. Product release is a critical step in HRPKS function to ensure timely termination and enzyme turnover. Nearly all of the HRPKSs characterized to date employ a separate thioesterase (TE) or acyltransferase enzyme for product release. In this study, we characterized two fungal HRPKSs that have fused C-terminal TE domains, a new domain architecture for fungal HRPKSs. We showed that both HRPKS-TEs synthesize aminoacylated polyketides in an ATP-independent fashion. The KU42 TE domain selects cysteine and homocysteine, and catalyzes transthioesterification using the side chain thiol group as the nucleophile. In contrast, the KU43 TE domain selects leucine methyl ester and performs a direct amidation of the polyketide, a reaction typically catalyzed by nonribosomal peptide synthetase (NRPS) domains. The characterization of these HRPKS-TE enzymes showcase the functional diversity of HRPKS enzymes, and provides potential TE domains as biocatalytic tools to diversify HRPKS structures.

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Section: Resultsmentioning

confidence: 99%

“…18 It was proposed that the thioester intermediate is at a higher ground state energy compared to the oxyester, and thus is favorable in driving β-lactone formation. 18…”

Section: Resultsmentioning

confidence: 99%

Section: Ku42 Hrpks-te Substrate Scope and Proposed Reaction Mechanismmentioning

confidence: 93%

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