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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry represents the AA14 family of lytic polysaccharide monooxygenases (LPMOs), mainly found in fungi. These enzymes cleave polysaccharides through an oxidative, instead of hydrolytic, mechanism. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H2O2 or O2 as a cosubstrate [ ]. For instance, AA14 family lytic polysaccharide monooxygenase A, is a lytic polysaccharide monooxygenase (LPMO) that has a broad substrate specificity with strong oxidative activity on pure amorphous cellulose and xyloglucan and plays as a bifunctional enzyme to decompose some specific network structures formed between cellulose and hemicellulose in the plant cell walls []. It simultaneously oxidizes cellulose, xylan and xyloglucan in natural hemi/cellulosic substrate such as fibrillated eucalyptus pulp, and releases native and oxidized cello-oligosaccharides, xylo-oligosaccharides and xyloglucan oligosaccharides from this substrate [].Proteins in this entry fold into a globular structure, the core of which comprising largely an Ig-like β-sandwich [ ]. The active site consists of two histidine and a tyrosine residue, forming the canonical histidine brace exposed at the surface. | Name | Lytic polysaccharide monooxygenase AA14 |
| Short Name | LPMO_AA14 | Type | Family |
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