ArticleChemical communications (Cambridge, England)2017
In trans hydrolysis of carrier protein-bound acyl intermediates by CitA during citrinin biosynthesis.
Article in Chemical communications (Cambridge, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022Article
- Core Steps to the Azaphilone Family of Fungal Natural Products.Chembiochem : a European journal of chemical biology · 2021Review
- A proof-reading mechanism for non-proteinogenic amino acid incorporation into glycopeptide antibiotics.Chemical science · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Polyketide synthases (PKSs) have several known editing mechanisms to ensure that non-productive intermediates are removed from the acyl carrier protein (ACP). We demonstrate that CitA, a putative hydrolase in the citrinin biosynthetic gene cluster, removes ACP-bound acyl intermediates. We propose that it serves an editing role in trans.
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