Literature summary for 3.4.21.25 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 .

Search for more literature for 3.4.21.25

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Cucumis melo	-	-

Organism

Organism	UniProt	Comment	Textmining
Cucumis melo	Q39547	-	-

Purification (Commentary)

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
fruit	-	Cucumis melo	-

Substrates and Products (Substrate)

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

Subunits

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

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Release 2023.1 (January 2023)