The Enzyme Database

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EC 3.4.23.39     
Accepted name: plasmepsin II
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-Phe┼Phe(NO2)-Ser-Phe-Pro-Thr [3]
Other name(s): 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, MetaCyc, MEROPS, 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]
[EC 3.4.23.39 created 1995]
 
 


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