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Literature summary for 3.5.1.103 extracted from

  • Huang, X.; Hernick, M.
    Examination of mechanism of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) reveals unexpected role for dynamic tyrosine (2012), J. Biol. Chem., 287, 10424-10434.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D146A below 0.4% of wild-type activity Mycolicibacterium smegmatis
D15A 0.5% of wild-type activity Mycolicibacterium smegmatis
H144A 1.0% of wild-type activity Mycolicibacterium smegmatis
Y142A 6.8% of wild-type activity Mycolicibacterium smegmatis
Y142F 5.3% of wild-type activity Mycolicibacterium smegmatis
Y142Q 5.9% of wild-type activity Mycolicibacterium smegmatis

Inhibitors

Inhibitors Comment Organism Structure
NaF uncompetitive inhibitor, consistent with a metal-water/hydroxide functioning as the reactive nucleophile in the catalytic mechanism Mycolicibacterium smegmatis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
9
-
N-acetyl-D-glucosamine mutant Y142F, pH 7.5, 30┬░C Mycolicibacterium smegmatis
17
-
N-acetyl-D-glucosamine mutant Y142Q, pH 7.5, 30┬░C Mycolicibacterium smegmatis
22
-
N-acetyl-D-glucosamine mutant Y142A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
38
-
N-acetyl-D-glucosamine wild-type, pH 7.5, 30┬░C Mycolicibacterium smegmatis
52
-
N-acetyl-D-glucosamine mutant D15A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
57
-
N-acetyl-D-glucosamine mutant H144A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
400
-
N-acetyl-D-glucosamine above 400 mM, mutant D146A, pH 7.5, 30┬░C Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 general acid-base pair mechanism with the side chain of Asp-15 functioning as the general base catalyst and His-144 serving as the general acid catalyst, whereas the side chain of Tyr-142 probably assists in polarizing substrate/stabilizing the oxyanion intermediate. Tyr-142 is a dynamic side chain that plays key roles in catalysis, modulating substrate binding, chemistry, and product release Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-glucosamine + H2O
-
Mycolicibacterium smegmatis D-glucosamine + acetate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0048
-
N-acetyl-D-glucosamine mutant D15A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.0095
-
N-acetyl-D-glucosamine mutant Y142F, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.0115
-
N-acetyl-D-glucosamine mutant H144A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.02
-
N-acetyl-D-glucosamine mutant Y142Q, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.03
-
N-acetyl-D-glucosamine mutant Y142A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.0333
-
N-acetyl-D-glucosamine mutant D146A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.77
-
N-acetyl-D-glucosamine wild-type, pH 7.5, 30┬░C Mycolicibacterium smegmatis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00009
-
N-acetyl-D-glucosamine mutant D15A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.0002
-
N-acetyl-D-glucosamine mutant H144A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.00105
-
N-acetyl-D-glucosamine mutant Y142F, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.00117
-
N-acetyl-D-glucosamine mutant Y142Q, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.00136
-
N-acetyl-D-glucosamine mutant Y142A, pH 7.5, 30┬░C Mycolicibacterium smegmatis
0.2
-
N-acetyl-D-glucosamine wild-type, pH 7.5, 30┬░C Mycolicibacterium smegmatis