EC Number   |
Natural Substrates |
|---|
   3.4.24.84 | a-factor + H2O |
- |
| 3.4.24.84 | a-factor-CaaX + H2O |
- |
| 3.4.24.84 | METP-(639aa)-RSYLLGNSSPRTQSPQNC(farnesyl)-OCH3 + H2O |
- |
| 3.4.24.84 | prelamin A + H2O |
- |
| 3.4.24.84 | prelamin A + H2O |
cleavage occurs between the farnesylated cysteine and the A1 position of the CAAX motif, although the prelamin A peptide is predominantly cleaved between A1 and A2 |
| 3.4.24.84 | a-factor-CaaX + H2O |
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif |
| 3.4.24.84 | a-factor-CaaX + H2O |
removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A,V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position |
| 3.4.24.84 | a-factor + H2O |
Ste24 is required for the first of the two N-terminal processing steps of mating pheromone a-factor |
| 3.4.24.84 | a-factor + H2O |
Ste24 participates in both N- and C-terminal processing steps of a-factor |
