TY - JOUR
T1 - Recent insights into copper-containing lytic polysaccharide mono-oxygenases
AU - Hemsworth, G.R.
AU - Davies, G.J.
AU - Walton, P.H.
PY - 2013/10/1
Y1 - 2013/10/1
N2 - 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 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.
AB - 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 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.
UR - http://www.scopus.com/inward/record.url?scp=84885472701&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2013.05.006
DO - 10.1016/j.sbi.2013.05.006
M3 - Article
AN - SCOPUS:84885472701
SN - 0959-440X
VL - 23
SP - 660
EP - 668
JO - CURRENT OPINION IN STRUCTURAL BIOLOGY
JF - CURRENT OPINION IN STRUCTURAL BIOLOGY
IS - 5
ER -