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Results 1 - 5 of 5
EC Number
Posttranslational Modification
proteolytic modification
automaturation of proPfPM1 K110pN mutant at pH 4.0-4.5, with reduction of molecular weight by 5 kDa
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 4.0–5.5, which occurrs at Leu116P–Ser117P, seven residues upstream of the native cleavage site (Gly123P-Asn1)
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
proteolytic modification
proplasmepsin maturation appears to require acidic conditions, proplasmepsin maturation may not be autocatalytic in vivo
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
Results 1 - 5 of 5