期刊
DALTON TRANSACTIONS
卷 45, 期 42, 页码 16904-16912出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c6dt02793h
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资金
- BBSRC [BB/I014802/1, BB/L000423, BB/L021633/1]
- Biotechnology and Biological Sciences Research Council [BB/I014802/1, BB/L021633/1, 1511826] Funding Source: researchfish
The enzymatic deconstruction of recalcitrant polysaccharide biomass is central to the conversion of these substrates for societal benefit, such as in biofuels. Traditional models for enzyme-catalysed polysaccharide degradation involved the synergistic action of endo-, exo- and processive glycoside hydrolases working in concert to hydrolyse the substrate. More recently this model has been succeeded by one featuring a newly discovered class of mononuclear copper enzymes: lytic polysaccharide mono-oxygenases (LPMOs; classified as Auxiliary Activity (AA) enzymes in the CAZy classification). In 2013, the structure of an LPMO from Bacillus amyloliquefaciens, BaAA10, was solved with the Cu centre photo-reduced to Cu(I) in the X-ray beam. Here we present the catalytic activity of BaAA10. We show that it is a chitin-active LPMO, active on both alpha and beta chitin, with the Cu(II) binding with low nM K-D, and the substrate greatly increasing the thermal stability of the enzyme. A spiral data collection strategy has been used to facilitate access to the previously unobservable Cu(II) state of the active centre, revealing a coordination geometry around the copper which is distorted from axial symmetry, consistent with the previous findings from EPR spectroscopy.
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