KEGG   ENZYME: 3.4.23.38Help
Entry
EC 3.4.23.38                Enzyme                                 

Name
plasmepsin I;
aspartic hemoglobinase I;
PFAPG;
malaria aspartic hemoglobinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of the -Phe33!Leu- bond in the alpha-chain of hemoglobin, leading to denaturation of the molecule
Comment
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 3.4.23.6
History
EC 3.4.23.38 created 1995
Orthology
K06007  
plasmepsin I
Genes
PFA: 
PFH: 
Taxonomy
Reference
1  [PMID:2007860]
  Authors
Goldberg DE, Slater AF, Beavis R, Chait B, Cerami A, Henderson GB.
  Title
Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease.
  Journal
J. Exp. Med. 173 (1991) 961-9.
  Sequence
[pfa:PF14_0076]
Reference
2  [PMID:8313875]
  Authors
Francis SE, Gluzman IY, Oksman A, Knickerbocker A, Mueller R, Bryant ML, Sherman DR, Russell DG, Goldberg DE.
  Title
Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase.
  Journal
EMBO. J. 13 (1994) 306-17.
  Sequence
[pfa:PF14_0076]
Reference
3  [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.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
180189-87-1

DBGET integrated database retrieval system