Biochemistry division
Seminar title: "From histone deacetylase to nonribosomal peptides: structure, function, and biosynthesis"
Abstract:
Histone deacetylase 6 (HDAC6) is a promising drug target and is unique among all HDACs in that it contains tandem catalytic domains. Enzymological study of HDAC6 revealed the substrate specificity of each domain and the underlying structural basis. The understanding of structure-function relationship led to the discovery of HDAC10 as a polyamine deacetylase. Structural study also revealed the mode-of-action of the nonribosomal peptide HC toxin, which represents a family of naturally existing tetracyclic peptide HDAC inhibitors of fungal origin. Biosynthesis of fungal nonribosomal peptides in general and mechanistic study of nonlinear NRPS involved in fungal siderophore biosynthesis will be discussed. Three examples of an emerging family of single-module NRPS-like proteins will be presented. Uncovering the unique function of these proteins expanded the toolbox of biocatalysts and led to the discovery of new metabolism in biology.
