Title : Functional Characterization and Crystal Structure of the Bifunctional Thioesterase Catalyzing Epimerization and Cyclization in Skyllamycin Biosynthesis - Yu_2021_ACS.Catalysis_11_11733 |
Author(s) : Yu J , Juan S , Chi C , Liu T , Geng T , Cai Z , Dong W , Shi C , Ma X , Zhang Z , Xing B , Jin H , Zhang L , Dong S , Yang D , Ma M |
Ref : ACS Catal , 11 :11733 , 2021 |
Abstract :
The d-amino acid residues are hallmark building blocks of nonribosomal peptides. Here, we report the bifunctional thioesterase domain (TE domain) Skyxy-TE that catalyzes both epimerization and cyclization in skyllamycin biosynthesis. Skyxy-TE specifically catalyzes the epimerization of the C-terminal l-amino acid residue of the linear substrate, then catalyzes regioselective intramolecular cyclization. The crystal structure of Skyxy-TE was solved at 2.25 and site-directed mutagenesis was performed, revealing key residues involved in the epimerization and cyclization. This study expands the understanding of the versatile TE domains and facilitates chemoenzymatic synthesis or combinatorial biosynthesis in the future. |
PubMedSearch : Yu_2021_ACS.Catalysis_11_11733 |
PubMedID: |
Gene_locus related to this paper: strsq-a0a1j0r317 |
Substrate | Skyllamycin-A Skyllamycin-like-precursor |
Gene_locus | Skyllamycin-A Skyllamycin-like-precursor strsq-a0a1j0r317 |
Structure | Skyllamycin-A Skyllamycin-like-precursor strsq-a0a1j0r317 7DXO 7CRN |
Yu J, Juan S, Chi C, Liu T, Geng T, Cai Z, Dong W, Shi C, Ma X, Zhang Z, Xing B, Jin H, Zhang L, Dong S, Yang D, Ma M (2021)
Functional Characterization and Crystal Structure of the Bifunctional Thioesterase Catalyzing Epimerization and Cyclization in Skyllamycin Biosynthesis
ACS Catal
11 :11733
Yu J, Juan S, Chi C, Liu T, Geng T, Cai Z, Dong W, Shi C, Ma X, Zhang Z, Xing B, Jin H, Zhang L, Dong S, Yang D, Ma M (2021)
ACS Catal
11 :11733