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3.2.1.146: beta-galactofuranosidase

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

Word Map on EC 3.2.1.146

Reaction

beta-D-(1->5) galactofuranose tetramer
+
H2O
=
beta-D-(1->5) galactofuranose trimer
 +
D-galactose

Synonyms

Araf-ase, beta-D-galactofuranosidase, beta-D-galactofuranosidase 1, beta-D-galactofuranosidase 2, beta-D-galactofuranosidase 3, beta-D-galactofuranosidase 4, beta-galactofuranosidase, exo beta-D-galactofuranosidase, exo-beta-D-galactofuranosidase, exo-beta-galactofuranosidase, galactofuranose-specific beta-D-galactofuranosidase, Galf-ase, Galf-specific Galf-ase, Galf-specific hydrolase, More, ORF0232, ORF0643, ORF1110, ORF2125, ORF2812

ECTree

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

Engineering

Engineering on EC 3.2.1.146 - beta-galactofuranosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D183A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D201A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D330A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D336A
site-directed mutagenesis, the mutant shows equal activity as the wild-type enzyme
D372A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D386A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D414A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D423A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D482A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D500A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D508A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D590A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D602A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
E405A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E464A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E530A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E592A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E594A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D201A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D330A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D336A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows equal activity as the wild-type enzyme
-
D386A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
E464A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
additional information
truncation of the PA14 domain of the enzyme (N-terminal 179 amino acid residues), ORF0643 Galf-ase lacking the PA14 domain exhibits about half activity compared with full-length ORF0643