Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 23, Issue 5, Pages 660-668Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2013.05.006
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Funding
- Biotechnology and Biological Sciences Research Council [BB/I014802/1] Funding Source: researchfish
- BBSRC [BB/I014802/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I014802/1] Funding Source: Medline
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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 beta-sandwich folds containing an active site with a metal coordinated by an N-terminal histidine. Following some initial confusion about the identity of the metal ion it has now been shown that these enzymes are copper-dependent oxygenases. Here we assess recent developments in the academic literature, focussing on the structures of the copper active sites. We provide critical comparisons with known small-molecules studies of copper-oxygen complexes and with copper methane monoxygenase, another of nature's powerful copper oxygenases.
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