3.4.23.39: plasmepsin II

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For detailed information about plasmepsin II, go to the full flat file.

Reaction

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 =

Synonyms

AH II, aspartic hemoglobinase II, malarial aspartic protease, PFAPD, pfpm2, plasmepsin 2, plasmepsin II, PLm II, PLMII, PM II, PMII, PSM2

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.39 plasmepsin II

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Results	in table
7	AA Sequence
4	Application
1	CAS Registry Number
14	Cloned(Commentary)
14	Crystallization (Commentary)
2	General Information
294	IC50 Value
565	Inhibitors
3	kcat/KM [mM/s]
192	Ki Value [mM]
98	KM Value [mM]
11	Localization
3	Molecular Weight [Da]
15	Natural Substrates/ Products (Substrates)
65	Organism
1	Pathway
53	PDB ID
11	pH Optimum
4	pH Range
10	Posttranslational Modification
16	Protein Variants
13	Purification (Commentary)
1	Reaction
1	Reaction Type
65	Reference
1	Renatured (Commentary)
4	Source Tissue
99	Substrates and Products (Substrate)
7	Subunits
36	Synonyms
6	Temperature Optimum [°C]
102	Turnover Number [1/s]

Renatured

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

differential scanning calorimetry reveals that the native state of PMII is irreversibly unfolded, and in the pH range of 6.5-8.0, PMII refolds to a denatured state with higher thermal stability than native state. The denatured state can also be formed upon partially unfolding PMII at pH 11.0 and 37°C for 2 h, followed by adjustment to a pH in the range of 6.5-8.0. While the denatured state can be folded/unfolded reversibly, the native state exists as a kinetically trapped state. The native state is kinetically trapped by an unfolding barrier of 25.5 kcal/mol, and yet once unfolded, is prevented from folding by a comparable folding barrier

Plasmodium falciparum

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717158