Literature summary for 3.4.24.25 extracted from

Iqbal, A.; Azim, M.K.; Hashmi, N.; Ali, S.A.; Musharaf, S.G.
Structural characterization of metalloprotease vibriolysin of cholera pathogen Vibrio cholerae (2011), Protein Pept. Lett., 18, 287-294.

Search for more literature for 3.4.24.25

Cloned(Commentary)

Cloned (Comment)	Organism
expression of pro-vibriolysin in Escherichia coli and cleavage of the N-terminal propeptide	Vibrio cholerae serotype O1

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	a zinc metalloprotease	Vibrio cholerae serotype O1

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
35000	-	x * 45000, pro-vibriolysin, SDS-PAGE, x * 35000, vibriolysin, SDS-PAGE	Vibrio cholerae serotype O1
45000	-	x * 45000, pro-vibriolysin, SDS-PAGE, x * 35000, vibriolysin, SDS-PAGE	Vibrio cholerae serotype O1

Organism

Organism	UniProt	Comment	Textmining
Vibrio cholerae serotype O1	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	recombinant pro-vibriolysin is cleaved to the 35 kDA mature vibriolysin	Vibrio cholerae serotype O1

Purification (Commentary)

Purification (Comment)	Organism
recombinant processed 35 kDa vibriolysin from Escherichia coli by anion exchange chromatography and gel filtration to homogeneity	Vibrio cholerae serotype O1

Subunits

Subunits	Comment	Organism
?	x * 45000, pro-vibriolysin, SDS-PAGE, x * 35000, vibriolysin, SDS-PAGE	Vibrio cholerae serotype O1
More	alpha and beta secondary structure analysis, circular dichroism, overview	Vibrio cholerae serotype O1

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Release 2023.1 (January 2023)