Literature summary extracted from

Bujacz, A.; Jedrzejczak-Krzepkowska, M.; Bielecki, S.; Redzynia, I.; Bujacz, G.
Crystal structures of the apo form of beta-fructofuranosidase from Bifidobacterium longum and its complex with fructose (2011), FEBS J., 278, 1728-1744.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.2.1.26	expression in Escherichia coli	Bifidobacterium longum

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.2.1.26	apo form of beta-fructofuranosidase and its complex with fructose, both to 1.8 A resolution. Enzyme consists of the N-terminal five-blade beta-propeller domain that includes the catalytic site, as well as the beta-sandwich C-terminal domain. The active site is located at the bottom of the axial funnel created by the interblade loops and the loops between beta-strand 2-3 of each blade. The protein has a 35-residue elongation of the N-terminus containing a fiveturn alpha-helix, which distinguishes it from the other known members of the GH32 family	Bifidobacterium longum

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
3.2.1.26	59156	-	x * 59156, calculated for recombinant protein. x * 60000, SDS-PAGE	Bifidobacterium longum
3.2.1.26	60000	-	x * 59156, calculated for recombinant protein. x * 60000, SDS-PAGE	Bifidobacterium longum

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.2.1.26	Bifidobacterium longum	A2TLS9	-	-

Subunits

EC Number	Subunits	Comment	Organism
3.2.1.26	?	x * 59156, calculated for recombinant protein. x * 60000, SDS-PAGE	Bifidobacterium longum

pI Value

EC Number	Organism	Comment	pI Value Maximum	pI Value
3.2.1.26	Bifidobacterium longum	calculated	-	4.9

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Release 2023.1 (January 2023)