3.4.24.84 a-factor + H2O - Arabidopsis thaliana fragments of a-factor - ? 355679 3.4.24.84 a-factor + H2O mating pheromone a-factor Saccharomyces cerevisiae fragments of a-factor - ? 355679 3.4.24.84 a-factor + H2O complements yeast ste24DELTA mutant Homo sapiens fragments of a-factor - ? 355679 3.4.24.84 a-factor + H2O Ste24 participates in both N- and C-terminal processing steps of a-factor Homo sapiens fragments of a-factor - ? 355679 3.4.24.84 a-factor + H2O Ste24 participates in both N- and C-terminal processing steps of a-factor Saccharomyces cerevisiae fragments of a-factor - ? 355679 3.4.24.84 a-factor + H2O mutant a-factor, containing a A8G point mutation is not cleaved suggesting that Ste24 N-terminal protease activity is highly discriminating Saccharomyces cerevisiae fragments of a-factor - ? 355679 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 Saccharomyces cerevisiae fragments of a-factor - ? 355679 3.4.24.84 a-factor + H2O - Homo sapiens ? - ? 384025 3.4.24.84 a-factor + H2O the enzyme has CAAX endopeptidase activity towards a-factor substrate Homo sapiens ? - ? 384025 3.4.24.84 a-factor mating pheromone + H2O - Saccharomyces mikatae ? - ? 449412 3.4.24.84 a-factor-CaaX + H2O - Homo sapiens a-factor-C + aaX - ? 366727 3.4.24.84 a-factor-CaaX + H2O - Saccharomyces mikatae a-factor-C + aaX - ? 366727 3.4.24.84 a-factor-CaaX + H2O - Saccharomyces cerevisiae a-factor-C + aaX endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif ? 366727 3.4.24.84 a-factor-CaaX + H2O endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CAAX motif, enzyme may also play a role in amino-terminal proteolytic processing of a-factor Saccharomyces cerevisiae a-factor-C + aaX - ? 366727 3.4.24.84 a-factor-CaaX + H2O endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif Saccharomyces cerevisiae a-factor-C + aaX - ? 366727 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 Saccharomyces cerevisiae a-factor + aaX - ? 367536 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 Saccharomyces cerevisiae a-factor + aaX - ? 367536 3.4.24.84 Abeta 1-40 + H2O - Saccharomyces mikatae ? - ? 449415 3.4.24.84 Abz-K-SKTKC(farnesyl)VI(-dinitrophenyl derivative of lysine) + H2O - Homo sapiens ? - ? 449449 3.4.24.84 Abz-KSKTKC(farnesyl)VIKD + H2O - Saccharomyces mikatae ? - ? 449451 3.4.24.84 Abz-SEKKDNYIIKGV-(4-nitro)-Y + H2O - Saccharomyces mikatae ? - ? 449464 3.4.24.84 bovine insulin chain A chain + H2O - Saccharomyces mikatae ? - ? 449709 3.4.24.84 bovine insulin chain B chain + H2O - Saccharomyces mikatae ? - ? 449710 3.4.24.84 CaM53 + H2O CaM53 is a prenylated C2+-calmodulin from petunia Arabidopsis thaliana fragments of CaM53 - ? 355681 3.4.24.84 DAEFRHDSGYEVHHQK-(Dabcyl)-LVFFAE-(Edans)-DVGSNK + H2O - Saccharomyces mikatae ? - ? 449848 3.4.24.84 human insulin + H2O - Saccharomyces mikatae ? - ? 450056 3.4.24.84 K-Ras4b + H2O - Saccharomyces mikatae ? - ? 450098 3.4.24.84 METP-(639aa)-RSYLLGNSSPRTQSPQNC(farnesyl)-OCH3 + H2O - Homo sapiens METP-(639aa)-RSY + LLGNSSPRTQSPQNC(farnesyl)-OCH3 - ? 448772 3.4.24.84 additional information the enzyme does not cleave mutant prelamin A (L647R) Homo sapiens ? - ? 89 3.4.24.84 N-(Ac)-Cys-(farnesyl)-Ser-Ile-Met + H2O the enzyme can process the prelaminA-specific CAAX sequence Homo sapiens ? - ? 385229 3.4.24.84 prelamin A + H2O cleavage is dependent on processing at the CAAX-box Homo sapiens lamin A - ? 385579 3.4.24.84 prelamin A + H2O the enzyme removes the farnesylated tail of prelamin A Homo sapiens ? - ? 421217 3.4.24.84 prelamin A + H2O - Homo sapiens lamin A + ? - ? 434142 3.4.24.84 prelamin A + H2O - Homo sapiens lamin A + ? enzyme cleaves the prenylated and carboxylmethylated 15-amino acid tail from the C-terminus of prelamin A to yield mature lamin. Mutations in the lamin A gene that eliminate the ZMPSTE24 cleavage site lead to the premature aging disease Hutchinson-Gilford Progeria Syndrome ? 434142 3.4.24.84 prelamin A + H2O the C-terminal 41 amino acids of prelamin A contain sufficient context to allow cleavage of the tail by ZMPSTE24. Mutations in amino acids immediately surrounding the cleavage site (between Y646 and L647) interfere with efficient cleavage of the prelamin A tail, e,g R644C, L648A and N650A, in addition to L647R. 9 of the 15 residues within the cleaved tail that lie immediately upstream of the CAAX motif are not critical for ZMPSTE24-mediated cleavage, duplication of the same 9 amino acids impairs the ability of ZMPSTE24 to cleave prelamin A Homo sapiens lamin A + ? - ? 434142 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 Saccharomyces mikatae lamin A + ? - ? 434142 3.4.24.84 RACU88402 + H2O RACU88402 is a Rac-like GTPase Arabidopsis thaliana fragments of RACU88402 - ? 355682 3.4.24.84 trans,trans-farnesyl bromide + H2O - Saccharomyces mikatae ? - ? 450773 3.4.24.84 YIIKGVFWDPA(farnesyl)CVIA + H2O farnesylated 15-mer peptide containing the mature a-factor sequence and the native a-factor CAAX motif Saccharomyces cerevisiae YIIKGVFWDPA(farnesyl)C + Val-Ile-Ala - ? 355680 3.4.24.84 YIIKGVFWDPA[farnesyl-C]AMQ + H2O - Mus musculus YIIKGVFWDPA[farnesyl-C] + AMQ - ? 367538 3.4.24.84 YIIKGVFWDPA[farnesyl-C]VIA + H2O - Mus musculus YIIKGVFWDPA[farnesyl-C] + VIA - ? 367537