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3.5.1.103: N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase

This is an abbreviated version!
For detailed information about N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase, go to the full flat file.

Word Map on EC 3.5.1.103

Reaction

1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
+
H2O
=
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
 +
acetate

Synonyms

1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, 1-D-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, 1D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, AcGI deacetylase, GlcNAc-Ins deacetylase, GlcNAc-Ins-deacetylase, MshB, N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase, N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-D-glucopyranoside deacetylase, N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase, N-acetylglucosaminylinositol-deacetylase, Rv1170

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.103 N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase

Engineering

Engineering on EC 3.5.1.103 - N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D146A
D146N
the D146N mutant is about 10fold higher than that of the D146A mutant, suggesting that the ability to accept a hydrogen bond at this position contributes to GlcNAc substrate specificity. Because there does not appear to be a direct contact between Asp146 and substrate, this effect is likely mediated via positioning of other catalytically important residues. The mutant enzyme shows 3.7% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine
D15A
the mutant enzyme shows 0.5% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine
D95A
inactive mutant enzyme
E47A
the mutant enzyme shows 300% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine. Mutation decreases the value of KM GlcNAc (2-fold) and increases the value of kcat/KM GlcNAc (3-fold)
F216A
the mutant enzyme shows 110% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine
L19A
the mutant enzyme shows 115% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine
M98A
the mutant enzyme shows 15% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine
R68A
inactive mutant enzyme
D146A
D146N
-
the D146N mutant is about 10fold higher than that of the D146A mutant, suggesting that the ability to accept a hydrogen bond at this position contributes to GlcNAc substrate specificity. Because there does not appear to be a direct contact between Asp146 and substrate, this effect is likely mediated via positioning of other catalytically important residues. The mutant enzyme shows 3.7% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine
-
E47A
-
the mutant enzyme shows 300% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine. Mutation decreases the value of KM GlcNAc (2-fold) and increases the value of kcat/KM GlcNAc (3-fold)
-
D146A
-
below 0.4% of wild-type activity
D15A
-
0.5% of wild-type activity
H144A
-
1.0% of wild-type activity
Y142A
-
6.8% of wild-type activity
Y142F
-
5.3% of wild-type activity
Y142Q
-
5.9% of wild-type activity
additional information