Cargando…
Methyltransferases excised from trans-AT polyketide synthases operate on N-acetylcysteamine-bound substrates
Autores principales: | Stevens, D. Cole, Wagner, Drew T., Manion, Hannah R., Alexander, Bradley K., Keatinge-Clay, Adrian T. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4963292/ https://www.ncbi.nlm.nih.gov/pubmed/27301661 http://dx.doi.org/10.1038/ja.2016.66 |
Ejemplares similares
-
Quantification of N-acetylcysteamine activated methylmalonate incorporation into polyketide biosynthesis
por: Klopries, Stephan, et al.
Publicado: (2013) -
A Double-Hotdog with a New Trick: Structure and Mechanism
of the trans-Acyltransferase Polyketide Synthase
Enoyl-isomerase
por: Gay, Darren C., et al.
Publicado: (2014) -
An in vitro platform for engineering and harnessing modular polyketide synthases
por: Miyazawa, Takeshi, et al.
Publicado: (2020) -
Divergence of multimodular polyketide synthases revealed by a didomain structure
por: Zheng, Jianting, et al.
Publicado: (2012) -
Assessing and harnessing updated polyketide synthase modules through combinatorial engineering
por: Ray, Katherine A., et al.
Publicado: (2023)