Vincent A. McKie

TL;DR: Arabinanase Arb43A is the first enzyme known to display this topology as mentioned in this paper, revealing a five-bladed beta-propeller fold and a long V-shaped surface groove, partially enclosed at one end, formed a single extended substrate-binding surface across the face of the propeller.

TL;DR: Flexible ligand recognition targets the anaerobic fungal complex to a range of different components in the plant cell wall and thus plays a pivotal role in the highly efficient degradation of this composite structure by the microbial eukaryote.

TL;DR: Functional analyses of mannanase 26A, informed by the crystal structure of the enzyme, provided important insights into the role of residues close to the catalytic glutamates, showing that Trp-360 played a critical role in binding substrate at the −1 subsite, whereas Tyr-285 was important to the function of the nucleophile catalyst.

TL;DR: It is proposed that ArbA is an arabinanase that exhibits both an endo- and an exo- mode of action in Pseudomonas fluorescens, and is placed in glycosyl hydrolase Family 43.

TL;DR: Data indicate that P. cellulosa expresses a membrane-bound GH51 arabinofuranosidase that plays a pivotal role in releasing arabinose from a range of polysaccharides and oligosaccharides.