Accepted name: plasmepsin I
Reaction: Hydrolysis of the -Phe33┼Leu- bond in the α-chain of hemoglobin, leading to denaturation of the molecule
Other name(s): aspartic hemoglobinase I; PFAPG; malaria aspartic hemoglobinase
Comments: Known from the malaria organism, Plasmodium. About 37 kDa. In peptidase family A1 (pepsin A family), closest to cathepsin D and renin in structure. Inhibited by pepstatin. Formerly included in EC
1.  Goldberg, D.E., Slater, A.F.G., Beavis, R., Chait, B., Cerami, A. and Henderson, G.B. Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease. J. Exp. Med. 173 (1991) 961–969. [PMID: 2007860]
2.  Francis, S.E., Gluzman, I.Y., Oksman, A., Knickerbocker, A., Mueller, R., Bryant, M.L., Sherman, D.R., Russell, D.G. and Goldberg, D.E. Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase. EMBO J. 13 (1994) 306–317. [PMID: 8313875]
3.  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]
[EC created 1995]

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