KEGG   ENZYME: 3.4.23.39Help
Entry
EC 3.4.23.39                Enzyme                                 

Name
plasmepsin II;
aspartic hemoglobinase II;
PFAPD
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
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]
Comment
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
Orthology
K06008  
plasmepsin II
Genes
PFA: 
PFH: 
Taxonomy
Reference
1  [PMID:7935597]
  Authors
Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C.
  Title
Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum.
  Journal
Mol. Biochem. Parasitol. 64 (1994) 177-90.
  Organism
Plasmodium falciparum [GN:pfa]
  Sequence
[pfa:PF14_0077]
Reference
2  [PMID:8163662]
  Authors
Gluzman IY, Francis SE, Oksman A, Smith CE, Duffin KL, Goldberg DE.
  Title
Order and specificity of the Plasmodium falciparum hemoglobin degradation pathway.
  Journal
J. Clin. Invest. 93 (1994) 1602-8.
  Organism
Plasmodium falciparum [GN:pfa]
Reference
3  [PMID:7925966]
  Authors
Hill J, Tyas L, Phylip LH, Kay J, Dunn BM, Berry C.
  Title
High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum.
  Journal
FEBS. Lett. 352 (1994) 155-8.
  Organism
Plasmodium falciparum [GN:pfa]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
159447-18-4

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