Crystallization (Comment) | Organism |
---|---|
molecular modeling. The conserved residue Glu99 is buried in the Met-S-(O) groove, which might contribute to the correct placing of substrates. Residue Asp134 does not form hydrogen bonds with the substrates but only within the enzyme | Aspergillus nidulans |
Protein Variants | Comment | Organism |
---|---|---|
D134E | most active among the mutant enzymes tested, less active than wild-type | Aspergillus nidulans |
D134N | lowest activity among all mutants tested for ac-L-Lys-L-Asn-l-Met(O)-L-Asp-L-Lys-dinitrophenol | Aspergillus nidulans |
E99Q | lowest activity towards all substrates tested except for ac-L-Lys-L-Asn-l-Met(O)-L-Asp-L-Lys-dinitrophenol | Aspergillus nidulans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus nidulans | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ac-L-Lys-L-Asn-L-Met(O)-L-Asp-L-Lys-dinitrophenol + dithiothreitol | - |
Aspergillus nidulans | ac-L-Lys-L-Asn-L-Met-L-Asp-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O | - |
? | |
ac-L-Lys-L-Asp-L-Met(O)-L-Asn-L-Lys-dinitrophenol + dithiothreitol | - |
Aspergillus nidulans | ac-L-Lys-L-Asp-L-Met-L-Asn-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O | - |
? | |
ac-L-Lys-L-Asp-L-Met(O)-L-Asp-L-Lys-dinitrophenol + dithiothreitol | - |
Aspergillus nidulans | ac-L-Lys-L-Asp-L-Met-L-Asp-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O | - |
? | |
ac-L-Lys-L-Phe-L-Met(O)-L-Lys-L-Lys-dinitrophenol + dithiothreitol | - |
Aspergillus nidulans | ac-L-Lys-L-Phe-L-Met-L-Lys-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O | - |
? |