Department of Chemistry, University of York, Heslington, York YO10 5DD, UK.
Curr Opin Struct Biol. 2013 Oct;23(5):660-8. doi: 10.1016/j.sbi.2013.05.006. Epub 2013 Jun 14.
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.
最近，发现了氧化酶在腐生细菌和真菌降解多糖中的作用，这对多糖降解仅通过水解途径的经典模型提出了挑战。细菌 AA10（以前的 CBM33）和真菌 AA9（以前的 GH61）裂解多糖单加氧酶的 3D 结构分析揭示了具有β-夹心折叠结构的酶，其中包含一个活性位点，该位点由 N 端组氨酸配位的金属离子协调。在最初对金属离子的身份有些困惑之后，现在已经表明这些酶是铜依赖性加氧酶。在这里，我们评估了学术文献中的最新进展，重点是铜活性位点的结构。我们与已知的铜-氧配合物的小分子研究以及另一种自然界强大的铜加氧酶——铜甲烷单加氧酶进行了批判性比较。
