EC Number   |
Reference |
|---|
   1.14.99.56 | comparison of isoforms LPMO9A, LPMO9B and LPMO9C. LPMO9B contains distal from the coordinated copper sphere an additional loop (Gly115-Asn121), which is not present in LPMO9A and LPMO9C. The copper ion in LPMO9A, LPMO9B and LPMO9C is coordinated by His1-His68-Tyr153, His1-His79-Tyr170 and His1-His84-Tyr166, respectively. All three LPMOs share two putative disulfide bridges |
740210 |
| 1.14.99.56 | hybrid quantum mechanics and molecular mechanics investigation of the first steps of the LPMO mechanism, which is reduction of Cu(II) to Cu(I) and the formation of a Cu(II)-superoxide complex. In the complex, the superoxide can bind either in an equatorial or an axial position. The equatorial isomer of the superoxide complex is over 60 kJ/mol more stable than the axial isomer because it is stabilized by interactions with a second-coordination-sphere glutamine residue |
743929 |
| 1.14.99.56 | single-molecule study by atomic force microscopy |
745866 |
| 1.14.99.56 | structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides |
745861 |
| 1.14.99.56 | structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry |
745380 |
| 1.14.99.56 | substrate cellohexaose binds to subsites ?4 to +2, and cellotriose from subsites -1 to +2. Residue Tyr203 is placed approximately 15 A away from the copper active site |
741041 |
