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3.2.1.38: beta-D-fucosidase

This is an abbreviated version!
For detailed information about beta-D-fucosidase, go to the full flat file.

Word Map on EC 3.2.1.38

Reaction

colanic acid
+
H2O
=
beta-D-fucopyranose
+
6-O-AcGlcbeta(1-4)[6-O-pyruvylGalbeta(1-4)GlcAbeta(1-3)Galbeta(1-3)]Fucbeta(1-4)Fucbeta-R

Synonyms

1,4-beta-fucoside hydrolase, beta-D-fucosidase, beta-D-fucoside fucohydrolase, beta-D-galactosidase/beta-D-fucosidase, beta-D-gluco/fuco/galactosidase, beta-D-glucosidase/beta-D-fucosidase, beta-fucosidase, beta-fucosidase I, beta-fucosidase II, BglMKg, colanase, FucA, M8 mutant of glycoside hydrolase GK3214, MeBglD2, More, Pb280, PRGH1

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.38 beta-D-fucosidase

Engineering

Engineering on EC 3.2.1.38 - beta-D-fucosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E205A
-
complete loss of activity
E239A
-
complete loss of activity
E205A
-
complete loss of activity
-
E239A
-
complete loss of activity
-
E173N
mutant enzyme shows no activity
E389N
mutant enzyme shows no activity
E446N
beta-fucosidase activity is 26.49% compared to wild-type activity, beta-glucosidase activity is 21.37% compared to wild-type activity, beta-galactosidase activity is 15.7% compared to wild-type activity
N172A
beta-fucosidase activity is 18.38% compared to wild-type activity, beta-glucosidase activity is 17.65% compared to wild-type activity, beta-galactosidase activity is 13.4% compared to wild-type activity
D206N
catalytically active mutant enzyme, similar temperature optimum like wild-type enzyme. The high-catalytic turn-over rate by D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures
D206Q
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
E207S
no hydrolytic activity
E399S
no hydrolytic activity
Q77R
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
additional information