Structure and specificity of a permissive bacterial C-prenyltransferase | Zendy

Sherif I. Elshahawi | Zendy; Hongnan Cao | Zendy; Khaled A. Shaaban | Zendy; Larissa V. Ponomareva | Zendy; Thangaiah Subramanian | Zendy; Mark Farman | Zendy; H. Peter Spielmann | Zendy; G.N. Phillips | Zendy; Jon S. Thorson | Zendy; Shanteri Singh | Zendy

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Structure and specificity of a permissive bacterial C-prenyltransferase

Author(s) -

Sherif I. Elshahawi,

Hongnan Cao,

Khaled A. Shaaban,

Larissa V. Ponomareva,

Thangaiah Subramanian,

Mark Farman,

H. Peter Spielmann,

G.N. Phillips,

Jon S. Thorson,

Shanteri Singh

Publication year - 2017

Publication title -

nature chemical biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.412

H-Index - 216

eISSN - 1552-4469

pISSN - 1552-4450

DOI - 10.1038/nchembio.2285

Subject(s) - prenyltransferase , prenylation , daptomycin , biochemistry , chemistry , farnesol , permissive , biology , enzyme , computational biology , bacteria , staphylococcus aureus , virology , vancomycin , genetics

This study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin. Two additional PTs also produced novel prenylated daptomycins with improved antibacterial activities over the parent drug.

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