EC Number   |
Reference |
|---|
   1.14.99.53 | molecular dynamics interactions between the LPMO and three different surface topologies of crystalline chitin. Most enzyme-substrate interactions involve the polysaccharide chain that is to be cleaved. Enzyme displays a constrained active site geometry as well as a tunnel connecting the bulk solvent to the copper site, through which only small molecules such as H2O, O2, and H2O2 can diffuse. Rearrangement of Cu-coordinating water molecules is necessary when binding the substrate and also provide a rationale for the experimentally observed C1 oxidative regiospecificity |
744375 |
| 1.14.99.53 | 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 |
| 1.14.99.53 | structures in the resting state and of a copper(II)-dioxo intermediate complex formed in the absence of substrate reveal pre-bound molecular oxygen adjacent to the active site. A conserved histidine is involved in promoting oxygen activation |
744034 |
| 1.14.99.53 | to 1.2 A resolution. Diffraction resolution and crystal morphology are improved by expression from a glycoengineered strain of Pichia pastoris |
743966 |
| 1.14.99.53 | to 1.3 A resolution |
741336 |
| 1.14.99.53 | to 1.85 A resolution, tri-modular enzyme containing a catalytic family AA10 LPMO module, a family 5 chitin-binding module, and a C-terminal unclassified module which displays tight and specific binding to chitin |
740758 |
