Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cyanide | substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide | Neurospora crassa |
Crystallization (Comment) | Organism |
---|---|
docking studies with cellulose hexamer. The surface patch surrounding the copper site appears to be a preferred interaction surface. Residue Tyr204 appears not to be involved in binding of this substrate | Neurospora crassa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | the copper ion alone hardly contributes to affinity, but substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide | Neurospora crassa | |
Zn2+ | Zn2+-shows slightly weaker binding compared with Cu2+ | Neurospora crassa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neurospora crassa | Q7SHI8 | - |
- |
Neurospora crassa DSM 1257 | Q7SHI8 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cellulose hexasaccharide + acceptor + O2 | - |
Neurospora crassa | ? + reduced acceptor + H2O | - |
? | |
cellulose hexasaccharide + acceptor + O2 | - |
Neurospora crassa DSM 1257 | ? + reduced acceptor + H2O | - |
? | |
additional information | substrate binding has a substantial effect on the chemical shifts of residues His1, Ala80, His83 and His155 | Neurospora crassa | ? | - |
? | |
additional information | substrate binding has a substantial effect on the chemical shifts of residues His1, Ala80, His83 and His155 | Neurospora crassa DSM 1257 | ? | - |
? | |
polymeric xyloglucan + acceptor + O2 | - |
Neurospora crassa | ? + reduced acceptor + H2O | - |
? | |
polymeric xyloglucan + acceptor + O2 | - |
Neurospora crassa DSM 1257 | ? + reduced acceptor + H2O | - |
? | |
xyloglucan 14-mer + acceptor + O2 | - |
Neurospora crassa | ? + reduced acceptor + H2O | - |
? | |
xyloglucan 14-mer + acceptor + O2 | - |
Neurospora crassa DSM 1257 | ? + reduced acceptor + H2O | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme acts in synergy with cellobiose dehydrogenase. The cytochrome domain of cellobiose dehydrogenase interacts with the copper site of the LPMO and substrate binding precludes interaction with cellobiose dehydrogenase | Neurospora crassa |