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3.2.1.86: 6-phospho-beta-glucosidase

This is an abbreviated version!
For detailed information about 6-phospho-beta-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.86

Reaction

6-phospho-beta-D-glucosyl-(1->4)-D-glucose
+
H2O
=
D-glucose
 +
D-glucose 6-phosphate

Synonyms

6-phospho-alpha-glucosidase, 6-phospho-beta-glucosidase, AscB protein, bgl-2, BglA, BglA-2, BglA3, bglD, BglT, CelD, Cellobiose-6-phosphate hydrolase, Gan1D, LacG1, LacG2, More, P-beta-glc, PalH, Pbgl25-217, phospho-alpha-glucosidase, phospho-beta-glucosidase, phospho-beta-glucosidase A, phosphocellobiase, SPD_0247, SPy1599

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.86 6-phospho-beta-glucosidase

Engineering

Engineering on EC 3.2.1.86 - 6-phospho-beta-glucosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E173S
site-directed mutagenesis
E173S/I174V
site-directed mutagenesis
I174V
site-directed mutagenesis
E173S
-
site-directed mutagenesis
-
E173S/I174V
-
site-directed mutagenesis
-
I174V
-
site-directed mutagenesis
-
C195G
the mutant shows significantly enhanced activity towards salicin compared to the wild type enzyme
W433A
the mutation shifts the enzyme specificity from dual activity to a significant preference toward 6-phospho-beta-glucosidase activity
W433M
the mutation shifts the enzyme specificity from dual activity to a significant preference toward 6-phospho-beta-glucosidase activity
E170Q
-
catalytic mutant
-
W433A
-
the mutation shifts the enzyme specificity from dual activity to a significant preference toward 6-phospho-beta-glucosidase activity
-
W433M
-
the mutation shifts the enzyme specificity from dual activity to a significant preference toward 6-phospho-beta-glucosidase activity
-
E182A
-
inactive mutant
E374A
-
inactive mutant
E171A
site-directed mutagenesis, inactive mutant
E171Q
site-directed mutagenesis, inactive mutant
E364A
site-directed mutagenesis, inactive mutant
E364Q
site-directed mutagenesis, inactive mutant
K430A
site-directed mutagenesis, inactive mutant
M423A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S424A
site-directed mutagenesis, inactive mutant
W338A
site-directed mutagenesis, inactive mutant
Y126A
site-directed mutagenesis, inactive mutant
Y126F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y303A
site-directed mutagenesis, inactive mutant
Y303F
site-directed mutagenesis, inactive mutant
Y432F
site-directed mutagenesis, inactive mutant
E179A
site-directed mutagenesis, inactive mutant
E372A
site-directed mutagenesis, inactive mutant
K435L
site-directed mutagenesis, inactive mutant
S427A
site-directed mutagenesis, the mutant shows slightly decreased activity but substrate affinities compared to the wild-type enzyme
S427C
site-directed mutagenesis, the mutant shows increased activity but substrate affinities compared to the wild-type enzyme
S427D
site-directed mutagenesis, almost inactive mutant
S427E
site-directed mutagenesis, almost inactive mutant
W420A
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
W420F
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Y311F
site-directed mutagenesis, inactive mutant
Y437F
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme