Reaction: Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves the small molecule substrates such as Ala-Leu-Glu-Arg-Thr-PhePhe(NO2)-Ser-Phe-Pro-Thr [3]
Other names: aspartic hemoglobinase II; PFAPD
Comments: Known from the malaria organism, Plasmodium. About 37 kDa. In peptidase family A1 (pepsin A family), and is 73% identical in sequence to plasmepsin I. Inhibited by pepstatin. Formerly included in EC 3.4.23.6
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 159447-18-4
References
1. Dame, J.B., Reddy, G.R., Yowell, C.A., Dunn, B.M., Kay, J. and Berry, C. Sequence, expression and modelled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 64 (1994) 177-190. [PMID: 7935597]
2. Gluzman, I.Y., Francis, S.E., Oksman, A., Smith, C.E., Duffin, K.L. and Goldberg, D.E. Order and specificity of the Plasmodium falciparum hemoglobin degradation pathway. J. Clin. Invest. 93 (1994) 1602-1608. [PMID: 8163662]
3. Hill, J., Tyas, L., Phylip, L.H., Kay, J., Dunn, B.M. and Berry, C. High level expression and characterisation of plasmepsin II, an aspartic proteinase from Plasmodium falciparum. FEBS Lett. 352 (1994) 155-158. [PMID: 7925966]