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Literature summary for 3.2.1.26 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bifidobacterium longum

Crystallization (Commentary)

Crystallization (Comment) Organism
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]

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

Organism

Organism UniProt Comment Textmining
Bifidobacterium longum A2TLS9
-
-

Subunits

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

pI Value

Organism Comment pI Value Maximum pI Value
Bifidobacterium longum calculated
-
4.9