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: PF3D7_1407900
PFH: PFHG_00464
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 173:961-9 (1991)
  Sequence
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 13:306-17 (1994)
  Sequence
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 93:1602-8 (1994)
DOI:10.1172/JCI117140
Other DBs
ExplorEnz - The Enzyme Database: 3.4.23.38
IUBMB Enzyme Nomenclature: 3.4.23.38
ExPASy - ENZYME nomenclature database: 3.4.23.38
BRENDA, the Enzyme Database: 3.4.23.38
CAS: 180189-87-1

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