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3.2.1.197: beta-1,2-mannosidase

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

Reaction

beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
+
H2O
=
beta-D-mannopyranosyl-(1->2)-D-mannopyranose
+
alpha-D-mannopyranose

Synonyms

BACOVA_03624, BT_3780, Dfer_3176

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.197 beta-1,2-mannosidase

Engineering

Engineering on EC 3.2.1.197 - beta-1,2-mannosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E227Q
32% of wild-type activity
E227Q/E268Q
no activity
E268A
5% of wild-type activity
E268Q
4% of wild-type activity
F344A
31% of wild-type activity
N74A
15% of wild-type activity
R89A
25% of wild-type activity
Y302A
6% of wild-type activity
E268A
-
5% of wild-type activity
-
E268Q
-
4% of wild-type activity
-
N74A
-
15% of wild-type activity
-
R89A
-
25% of wild-type activity
-
E224A
1.9% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
E265A
0.04% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
E224A
-
1.9% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
-
E265A
-
0.04% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
-