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Literature summary for 3.4.22.68 extracted from

  • Ponder, E.; Albrow, V.; Leader, B.; Bekes, M.; Mikolajczyk, J.; Fonovic, U.; Shen, A.; Drag, M.; Xiao, J.; Deu, E.; Campbell, A.; Powers, J.; Salvesen, G.; Bogyo, M.
    Functional characterization of a SUMO deconjugating protease of Plasmodium falciparum using newly identified small molecule inhibitors (2011), Chem. Biol., 18, 711-721.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.68

Cloned(Commentary)

Cloned (Comment) Organism
expression of the wild-type full-length PfSENP1 and the catalytic domain of PfSENP1 Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
3-[(4-[[2-([(2R,3R)-3-[benzyl(cyclohexa-1,3-dien-1-ylmethyl)carbamoyl]-3-chlorooxiran-2-yl]carbonyl)-2-(carboxymethyl)hydrazinyl]carbonyl]benzyl)carbamoyl]benzoic acid partial inhibition of the enzyme Plasmodium falciparum
3-[(4-[[2-[(2E)-4-[bis(naphthalen-1-ylmethyl)amino]-4-oxobut-2-enoyl]-2-(carboxymethyl)hydrazinyl]carbonyl]benzyl)carbamoyl]benzoic acid
-
 Plasmodium falciparum
3-[(4-[[2-[4-[bis(naphthalen-1-ylmethyl)amino]-2,3-dichloro-4-oxobutanoyl]-2-(carboxymethyl)hydrazinyl]carbonyl]benzyl)carbamoyl]benzoic acid the chlorohydrin form of JCP-666 may inhibit the target SENP by SN2-like displacement of the chloride by the active site cysteine Plasmodium falciparum
3-[(4-[[2-[4-[bis(naphthalen-1-ylmethyl)amino]-3-chloro-2-hydroxy-4-oxobutanoyl]-2-(carboxymethyl)hydrazinyl]carbonyl]benzyl)carbamoyl]benzoic acid i.e. JCP-666 Plasmodium falciparum
hSUMO-VS human SUMO protein modified with a vinyl sulfone reactive group after the C-terminal di-glycine, contains the full length SUMO protein fused to a reactive vinyl sulfone group, an irreversible inhibitor of SENP proteases Plasmodium falciparum
additional information inhibitor screening, overview. No inhibition by 3-[(4-[[2-[[(2R,3R)-3-(benzylcarbamoyl)-3-chlorooxiran-2-yl]carbonyl]-2-(carboxymethyl)hydrazinyl]carbonyl]benzyl)carbamoyl]benzoic acid, i.e. JCP-667 Plasmodium falciparum
N-ethylmaleimide NEM, blocks SENP activity by acting as a general alkylating agent that modifies the active site cysteine in parasite lysates Plasmodium falciparum
VEA-260
-
 Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
small ubiquitin-related modifier-protein + H2O Plasmodium falciparum SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins small ubiquitin-related modifier-protein + protein
-
 r

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information parasites in human red blood cells Plasmodium falciparum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PfSENP1 has unique substrate sequence specificity, comparison to human SENPs, mutational analysis, overview Plasmodium falciparum ?
-
 ?
small ubiquitin-related modifier-protein + H2O SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins Plasmodium falciparum small ubiquitin-related modifier-protein + protein
-
 r

Synonyms

Synonyms Comment Organism
PFL1635w
-
 Plasmodium falciparum
SENP
-
 Plasmodium falciparum
SENP1
-
 Plasmodium falciparum
SUMO deconjugating protease
-
 Plasmodium falciparum
SUMO-specific protease
-
 Plasmodium falciparum

General Information

General Information Comment Organism
evolution Plasmodium falciparum has only two predicted SENP proteases whereas human hosts have six SENPs Plasmodium falciparum