Arnling Baath_2019_J.Biol.Chem_294_6635

Reference

Title : Structure-function analyses reveal that a glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds - Arnling Baath_2019_J.Biol.Chem_294_6635
Author(s) : Arnling Baath J , Mazurkewich S , Poulsen JN , Olsson L , Lo Leggio L , Larsbrink J
Ref : Journal of Biological Chemistry , 294 :6635 , 2019
Abstract :

Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources. However, details on how GEs interact with their natural substrates are sparse, calling for thorough structure-function studies. Presented here is the structure and biochemical characterization of a GE, TtCE15A, from the bacterium Teredinibacter turnerae, a symbiont of wood-boring shipworms. To gain deeper insight into enzyme-substrate interactions, inhibition studies were performed with both the WT TtCE15A and variants in which we, by using site-directed mutagenesis, substituted residues suggested to have key roles in binding to or interacting with the aromatic and carbohydrate structures of its uronic acid ester substrates. Our results support the hypothesis that two aromatic residues (Phe-174 and Trp-376), conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The solved crystal structure of TtCE15A revealed features previously not observed in either fungal or bacterial GEs, with a large inserted N-terminal region neighboring the active site and a differently positioned residue of the catalytic triad. The findings highlight key interactions between GEs and complex lignin-carbohydrate ester substrates and advance our understanding of the substrate specificities of these enzymes in biomass conversion.

PubMedSearch : Arnling Baath_2019_J.Biol.Chem_294_6635
PubMedID: 30814248
Gene_locus related to this paper: tertt-c5bn23

Related information

Gene_locus tertt-c5bn23
Structure tertt-c5bn23    6HSW

Citations formats

Arnling Baath J, Mazurkewich S, Poulsen JN, Olsson L, Lo Leggio L, Larsbrink J (2019)
Structure-function analyses reveal that a glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds
Journal of Biological Chemistry 294 :6635

Arnling Baath J, Mazurkewich S, Poulsen JN, Olsson L, Lo Leggio L, Larsbrink J (2019)
Journal of Biological Chemistry 294 :6635