C81S |
no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing. Mutation does not change the charge or size of the amino acid side chain, but nevertheless greatly reduces activity |
Hevea brasiliensis |
E79A |
no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing. Mutation greatly reduces, but does not abolish activity. The negative charge provided by Glu-79 may be required in the active site, but a direct participation of this residue in enzyme catalysis is not suggested |
Hevea brasiliensis |
H10A |
mutation results in a 30000 Da protein with increased electrophoretic mobility on native high percentage (16%) polyacrylamide gels. the mutant enzyme displays almost wild-type specific activity in crude extracts, suggesting that His10 is not crucial for activity. However, activity is almost completely lost during purification, supporting the possibility that the H10A exchange has a destabilizing effect and may prevent formation of an active dimer of the enzyme after purification |
Hevea brasiliensis |
H235A |
inactive mutant enzyme, no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing |
Hevea brasiliensis |
S80A |
no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing |
Hevea brasiliensis |