EC Number   |
Protein Variants |
Reference |
|---|
   3.4.22.B71 | C548S |
catalytically inactive mutant |
716210 |
| 3.4.22.B71 | C548S |
site-directed mutagenesis, active site mutant |
732884 |
| 3.4.22.B71 | C549A |
catalytically inactive mutant |
715109 |
| 3.4.22.B71 | 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 |
732884 |
| 3.4.22.B71 | G545D |
slight decrease in SUMO-1 processing activity and SUMO-2 processing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate |
682080 |
| 3.4.22.B71 | G545F |
decrease in SUMO-1 processing activitya and SUMO-2 processing activity. Increase in SUMO-3 procesing activity |
682080 |
| 3.4.22.B71 | G545S |
decrease in SUMO-1 processing activity, SUMO-2 processing activity and SUMO-3 procesing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate |
682080 |
| 3.4.22.B71 | M497A |
increase in SUMO-1 processing activity and SUMO-3 procesing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate. Slight decrease in cleavage of the RanGAP1-SUMO-2/3 conjugate |
682080 |
| 3.4.22.B71 | M497L |
decrease in SUMO-1 processing activity, SUMO-2 processing activity and SUMO-3 procesing activity |
682080 |
| 3.4.22.B71 | M497N |
slight increase in SUMO-1 processing activity, decrease in SUMO-2 processing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate |
682080 |
