Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.2.1.153: fructan beta-(2,1)-fructosidase

This is an abbreviated version!
For detailed information about fructan beta-(2,1)-fructosidase, go to the full flat file.

Word Map on EC 3.2.1.153

Reaction

1,1,1,1-kestohexaose
+
H2O
=
1,1,1-kestopentaose
+
beta-D-fructofuranose

Synonyms

1-FEH, 1-FEH I, 1-FEH II, 1-FEH IIa, 1-FEH w1, 1-FEH w2, 1-FEH2a, 1-FEH2b, 1-FEHa, 1-FEHI, 1-FEHw1, 1-fructan exohydrolase, 1-fructoexohydrolase, beta-(2-1) fructan exohydrolase, beta-(2-1)-D-fructan fructohydrolase, beta-(2-1)-linkage specific FEH, beta-(2-1)-linkage specific fructan-beta-fructosidase, beta-(2-1)-linkage-specific fructan-beta-fructosidase, Ci1-FEH I, Ci1-FEH IIa, Ci1-FEH IIb, FEH, fructan 1-exohydrolase, fructan 1-exohydrolase I, fructan 1-exohydrolase IIa, fructan 1-exohydrolase IIb, fructan 1-exohydrolase w1, fructan 1-exohydrolase w2, fructan exohydrolase, fructanexohydrolase, Lp1-FEH, Lp1-FEHa, Wfh-sm3m

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.153 fructan beta-(2,1)-fructosidase

Crystallization

Crystallization on EC 3.2.1.153 - fructan beta-(2,1)-fructosidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method of recombinant enzyme heterologously expressed in Pichia pastoris. The structure of the isoenzyme 1-FEH IIa is determined at a resolution of 2.35 A. The structure consists of an N-terminal fivefold beta-propeller domain
-
hanging-drop vapour-diffusion method at 4°C. The crystals are tetragonal belonging to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 139.83, b = 139.83, c = 181.94 A
-