Crystallization (Comment) | Organism |
---|---|
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 | Serratia marcescens |
Protein Variants | Comment | Organism |
---|---|---|
Y54A | mutation of residue at subsite -4, minimal effect on degradation of beta-chitin, about 20% residual activity with substrate [(1->4)-N-acetyl-beta-D-glucosaminyl]6 | Serratia marcescens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | - |
Serratia marcescens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Serratia marcescens | O83009 | chitinase, cf. EC 3.2.1.14 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-chitin + ascorbate + O2 | - |
Serratia marcescens | C1-oxidized chitooligosaccharides + dehydroascorbate + H2O | - |
? | |
additional information | [(1->4)-N-acetyl-beta-D-glucosaminyl]6 is a substrate, but not shorter oligomers | Serratia marcescens | ? | - |
? | |
[(1->4)-N-acetyl-beta-D-glucosaminyl]6 + ascorbate + O2 | - |
Serratia marcescens | [(1->4)-N-acetyl-beta-D-glucosaminyl]3-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]2 + dehydroascorbate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AA10A | - |
Serratia marcescens |
CBP21 | - |
Serratia marcescens |