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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
Search for more literature for 3.5.1.103

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
a

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