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Literature summary extracted from

  • Sotokawauchi, A.; Kato-Murayama, M.; Murayama, K.; Hosaka, T.; Maeda, I.; Onjo, M.; Ohsawa, N.; Kato, D.I.; Arima, K.; Shirouzu, M.
    Structural basis of cucumisin protease activity regulation by its propeptide (2017), J. Biochem., 161, 45-53 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.25 expressed in Escherichia coli BL21-Gold (DE3) pLysS cells Cucumis melo

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.25 mature cucumisin-propeptide complex, sitting drop vapor diffusion method, using 0.05 M Bis-Tris buffer (pH 6.5) containing 0.05 M ammonium sulfate and 30% (w/v) pentaerythritol ethoxylate Cucumis melo

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.25 diisopropyl fluorophosphate
-
 Cucumis melo
3.4.21.25 additional information not inhibited by the C-terminal hepta-peptide of the propeptide (Asn-Glu-Met-Asn-Glu-Leu-His) Cucumis melo
3.4.21.25 propeptide 77.7% inhibition at 200 mM Cucumis melo

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.25 extracellular
-
 Cucumis melo
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.25 Cucumis melo Q39547
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.25 HiTrap chelating column chromatography and Superdex 200 gel filtration Cucumis melo

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.25 fruit
-
 Cucumis melo
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.25 glutaryl-alanyl-alanyl-prolyl-leucine-4-nitroanilide + H2O
-
 Cucumis melo glutaryl-alanyl-alanyl-prolyl-leucine + 4-nitroaniline
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.25 ? x * 67000, SDS-PAGE Cucumis melo