Structural highlights
Function
FCLN_PLAF7 In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:17074076). In the apicoplast, degrades apicoplast transit peptides after their cleavage (PubMed:17074076). Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (By similarity). At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (By similarity). At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (By similarity). The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (By similarity).[UniProtKB:A0A0L7KF24][1]
References
- ↑ Ponpuak M, Klemba M, Park M, Gluzman IY, Lamppa GK, Goldberg DE. A role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplast. Mol Microbiol. 2007 Jan;63(2):314-34. doi: 10.1111/j.1365-2958.2006.05443.x. Epub, 2006 Oct 27. PMID:17074076 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05443.x
