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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.38 plasmepsin I

Crystallization

Crystallization on EC 3.4.23.38 - plasmepsin I

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 PMI–KNI-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