Authors
Glyn R Hemsworth, Gideon J Davies, Paul H Walton
Publication date
2013/10/1
Source
Current opinion in structural biology
Volume
23
Issue
5
Pages
660-668
Publisher
Elsevier Current Trends
Description
Highlights
- Recently discovered polysaccharide mono-oxygenases are copper-containing enzymes.
- Different sequence families in bacteria and fungi are structurally similar but with subtle differences in active site and mechanism.
- Copper active sites use N-terminal histidine to coordinate to copper in the so-called ‘histidine brace’.
- Aided by these enzymes, recalcitrant biomass is becoming a viable biofuel source.
Recently the role of oxidative enzymes in the degradation of polysaccharides by saprophytic bacteria and fungi was uncovered, challenging the classical model of polysaccharide degradation of being solely via a hydrolytic pathway. 3D structural analyses of lytic polysaccharide mono-oxygenases of both bacterial AA10 (formerly CBM33) and fungal AA9 (formerly GH61) enzymes revealed structures with β-sandwich folds containing an active site with a metal coordinated by an N-terminal histidine. Following …
Scholar articles
GR Hemsworth, GJ Davies, PH Walton - Current opinion in structural biology, 2013