Crystallization (Comment) | Organism |
---|---|
recombinant chimeric mutant SENP2 C548S-loop1 in complex with SUMO2, X-ray diffraction structure determination and analysis at 2.15 A resolution | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C548S | site-directed mutagenesis, active site mutant | Homo sapiens |
F393G/K394G | construction of a chimeric enzyme SENP2 mutant with the insertion of loop1 from SENP6 into its sequence causing mutation of F393G/K394G, loop1 insertion is a determinant for SUMO2/3 activity and specificity, structure of SENP2-loop1 in complex with SUMO2, overview. The mutant reveals the details of an interface exclusive to SENP6/7 and the formation of unique contacts between both proteins, and the mutant shows an increase of the proteolytic activity for diSUMO2 and polySUMO2 substrates. The chimeric insertion mutant used for crystallization studies is also mutated at active site residue, C548S, for a stable complex formation | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9HC62 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant chimeric mutant SENP2 C548S-loop1 in complex with SUMO2 by gel filtration | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
diSUMO2 + H2O | - |
Homo sapiens | 2 SUMO2 | - |
? | |
polySUMO2 + H2O | - |
Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SENP2 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the SENP/ULP protease family | Homo sapiens |