3.4.23.38: plasmepsin I
This is an abbreviated version!
For detailed information about plasmepsin I, go to the full flat file.
Word Map on EC 3.4.23.38
-
3.4.23.38
-
plasmepsins
-
falciparum
-
plasmodium
-
malarial
-
antimalarial
-
cathepsin
-
vacuole
-
aspartyl
-
proteinases
-
hemoglobin-degrading
-
intraerythrocytic
-
autocatalytic
-
proplasmepsins
- 3.4.23.38
-
plasmepsins
- falciparum
- plasmodium
-
malarial
-
antimalarial
- cathepsin
- vacuole
-
aspartyl
- proteinases
-
hemoglobin-degrading
-
intraerythrocytic
-
autocatalytic
-
proplasmepsins
Reaction
hydrolysis of the -Phe33-/-Leu- bond in the alpha-chain of hemoglobin, leading to denaturation of the molecule =
Synonyms
AH I, aspartic hemoglobinase I, malaria aspartic hemoglobinase, PFAPG, PfPM1, plasmepsin 1, plasmepsin I, plasmepsin-I, PLm I, PM I, PM-I, PMI
ECTree
Advanced search results
Crystallization
Crystallization on EC 3.4.23.38 - plasmepsin I
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
recombinant PMI as apoenzyme and in complex with the potent peptidic inhibitor, (4R)-3-[(2S,3S)-3-{[(2,6-dimethylphenoxy)acetyl]amino}-2-hydroxy-4-phenylbutanoyl]-N-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide, i. e. KNI-10006, at the resolution of 2.4 and 3.1 A, respectively. The apoenzyme crystallizes in the orthorhombic space group P212121 with two molecules in the asymmetric unit. The KNI-10006 bound enzyme crystallized in the tetragonal space group P43 with four molecules in the asymmetric unit a. In the PMIKNI-10006 complex, the inhibitors are bound identically to all four enzyme molecules, with the opposite directionality of the main chain of KNI-10006 relative to the direction of the enzyme substrates