EC Number   |
Posttranslational Modification |
Reference  |
|---|
   3.4.23.38 | proteolytic modification |
the proenzyme has an unusually long propart of 125 amino acid residues that mediates type II membrane anchoring of the proenzyme, activation occurs by removal of the propart |
648182 |
| 3.4.23.38 | proteolytic modification |
proplasmepsin maturation appears to require acidic conditions, proplasmepsin maturation may not be autocatalytic in vivo |
648184 |
| 3.4.23.38 | proteolytic modification |
plasmepsin I is produced as a precursor. The propart region, about 120 residues, is more than twice as long as those of archetypal zymogens |
648190 |
| 3.4.23.38 | proteolytic modification |
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.0Β5.5, which occurrs at Leu116PΒSer117P, seven residues upstream of the native cleavage site (Gly123P-Asn1) |
682637 |
| 3.4.23.38 | proteolytic modification |
automaturation of proPfPM1 K110pN mutant at pH 4.0-4.5, with reduction of molecular weight by 5 kDa |
696329 |
