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1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
1-D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
key enzyme in mycothiol biosynthesis. Mycothiol is the major low molecular weight thiol in actinomycetes and is essential for growth of Mycobacterium tuberculosis
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-
?
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
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + H2O
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + acetate
-
-
-
?
cyclohexyl-2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside + H2O
cyclohexyl-2-amino-2-deoxy-1-thio-alpha-D-glucopyranoside + acetate
-
6% of the activity with 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
-
-
?
cyclohexyl-2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O
cyclohexyl-2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
-
6% of the activity with 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
-
-
?
N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + H2O
1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
-
-
-
?
N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-D-glucopyranoside + H2O
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + acetate
molecular docking analysis of the MshB active site binding pocket, overview
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?
N-acetyl-1D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + H2O
1D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
-
-
-
-
?
N-acetyl-D-glucosamine + H2O
acetate + D-glucosamine
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
N-deacetyl-N-formylmycothiol-monobromobimane conjugate + H2O
?
-
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-
?
phenyl 2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside + H2O
phenyl 2-amino-2-deoxy-1-thio-alpha-D-glucopyranoside + acetate
additional information
?
-
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
-
-
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
-
-
?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
-
-
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
-
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
-
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
biosynthesis of mycothiol
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
biosynthesis of mycothiol and detoxification of xenobiotics as their mycothiol-S-conjugates
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
key enzyme in mycothiol biosynthesis
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-
?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
step in mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
activity with 1-D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside as the substrate is over 300fold greater than the deacetylase activity determined with N-acety-D-glucosamine and 23fold greater than the amidase activity measured with MSmB
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
the enzyme is specific for 1-D-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
step in mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
biosynthesis of mycothiol
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
the enzyme is specific for 1-D-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
activity with 1-D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside as the substrate is over 300fold greater than the deacetylase activity determined with N-acety-D-glucosamine and 23fold greater than the amidase activity measured with MSmB
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
key enzyme in mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
the inositol moiety primarily contributes to the affinity of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside for MshB
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?
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
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?
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
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?
N-acetyl-D-glucosamine + H2O
acetate + D-glucosamine
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?
N-acetyl-D-glucosamine + H2O
acetate + D-glucosamine
commercially available alternate minimal substrate, MshB is 100fold less active towards this compound than toward the natural substrate
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?
N-acetyl-D-glucosamine + H2O
acetate + D-glucosamine
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
activity is 300fold lower than with 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
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-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
activity is 73fold lower than with 1-D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
activity is 300fold lower than with 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
activity is 73fold lower than with 1-D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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?
phenyl 2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside + H2O
phenyl 2-amino-2-deoxy-1-thio-alpha-D-glucopyranoside + acetate
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?
phenyl 2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside + H2O
phenyl 2-amino-2-deoxy-1-thio-alpha-D-glucopyranoside + acetate
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25% of the activity with 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
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?
additional information
?
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MshB shows amidase activity with a wide range of substrates
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?
additional information
?
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MshB shows amidase activity with a wide range of substrates
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?
additional information
?
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the enzyme is unable to remove the acetyl residue from the acetylcysteinyl group of mycothiol or S-(2-oxo-2-phenylethyl)mycothiol, and it exhibits barely detectable amidase activity with mycothiol or mycothiol disulfide. It has significant amidase activity with S-(2-oxo-2-phenylethyl)mycothiol and even greater activity with N-deacetyl-N-formylmycothiol-monobromobimane conjugate, N-deacetyl-mycothiol-monobromobimane conjugate, formyl-CySmB-GlcN-Ins, and mycothiol-monobromobimane conjugate
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?
additional information
?
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the enzyme is unable to remove the acetyl residue from the acetylcysteinyl group of mycothiol or S-(2-oxo-2-phenylethyl)mycothiol, and it exhibits barely detectable amidase activity with mycothiol or mycothiol disulfide. It has significant amidase activity with S-(2-oxo-2-phenylethyl)mycothiol and even greater activity with N-deacetyl-N-formylmycothiol-monobromobimane conjugate, N-deacetyl-mycothiol-monobromobimane conjugate, formyl-CySmB-GlcN-Ins, and mycothiol-monobromobimane conjugate
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?
additional information
?
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molecular determinants of MshB substrate specificity, docking analysis and simulations, a hydrophobic cavity adjacent to the active site may be one important determinant of MshB substrate specificity, the side chains of Asp15, His144, Asp146 and Tyr142 are important contributors to MshB catalytic activity, and Tyr142 appears to be a dynamic side chain that participates throughout the catalytic cycle, participating in substrate binding, chemistry, and product release
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additional information
?
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structural analogues of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-D-glucopyranoside in which the inosityl moiety is replaced by a chromophore are synthesized and evaluated as alternate substrates of MshB, assay method optimization for high-throughput measurements, molecular docking analysis of the MshB active site binding pocke, overview
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?
additional information
?
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structural analogues of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-D-glucopyranoside in which the inosityl moiety is replaced by a chromophore are synthesized and evaluated as alternate substrates of MshB, assay method optimization for high-throughput measurements, molecular docking analysis of the MshB active site binding pocke, overview
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?
additional information
?
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MshB shows amidase activity with a wide range of substrates
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?
additional information
?
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the enzyme is unable to remove the acetyl residue from the acetylcysteinyl group of mycothiol or S-(2-oxo-2-phenylethyl)mycothiol, and it exhibits barely detectable amidase activity with mycothiol or mycothiol disulfide. It has significant amidase activity with S-(2-oxo-2-phenylethyl)mycothiol and even greater activity with N-deacetyl-N-formylmycothiol-monobromobimane conjugate, N-deacetyl-mycothiol-monobromobimane conjugate, formyl-CySmB-GlcN-Ins, and mycothiol-monobromobimane conjugate
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additional information
?
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MshB activity as a control point regulating mycothiol production
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additional information
?
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MshB activity as a control point regulating mycothiol production
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?
additional information
?
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MshB activity as a control point regulating mycothiol production
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
1-D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
key enzyme in mycothiol biosynthesis. Mycothiol is the major low molecular weight thiol in actinomycetes and is essential for growth of Mycobacterium tuberculosis
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?
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + H2O
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + acetate
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?
N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + H2O
1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
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?
additional information
?
-
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
biosynthesis of mycothiol
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
biosynthesis of mycothiol and detoxification of xenobiotics as their mycothiol-S-conjugates
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
key enzyme in mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
-
mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
step in mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
step in mycothiol biosynthesis
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-
?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
biosynthesis of mycothiol
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
key enzyme in mycothiol biosynthesis
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?
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O
1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + acetate
mycothiol biosynthesis
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?
additional information
?
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MshB activity as a control point regulating mycothiol production
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?
additional information
?
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MshB activity as a control point regulating mycothiol production
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?
additional information
?
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MshB activity as a control point regulating mycothiol production
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
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enzyme has a strong preference for the Fe2+ cofactor under anaerobic conditions, regardless of the metal ion content of the medium. The preferred cofactor changes between Zn2+ and Fe2+ depending on the metal ion content of the medium when MshB is purified under aerobic conditions
Co2+
MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity
Co2+
MshB contains a divalent transition metal ion essential for activity. MshB isolated on the Ni-affinity column contains 0.36 equivalent of Ca and 0.82 equivalent of Ni, and less than 0.08 equivalent of Zn per subunit. MshB isolated on the Zn-affinity column contains less than 0.1 equivalent of Ca and 2.3 equivalents of Zn, and less than 0.08 equivalent of Ni per subunit. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity, but Ca2+ and Mg2+ produce no restoration of activity
Co2+
-
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+
Fe2+
the active site metal ion is coordinated to two histidine residues, His13 and His147, and an aspartate, Asp16
Fe2+
-
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+
Mn2+
MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity
Mn2+
MshB contains a divalent transition metal ion essential for activity. MshB isolated on the Ni-affinity column contains 0.36 equivalent of Ca and 0.82 equivalent of Ni, and less than 0.08 equivalent of Zn per subunit. MshB isolated on the Zn-affinity column contains less than 0.1 equivalent of Ca and 2.3 equivalents of Zn, and less than 0.08 equivalent of Ni per subunit. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity, but Ca2+ and Mg2+ produce no restoration of activity
Mn2+
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activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+
Ni2+
MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity
Ni2+
MshB contains a divalent transition metal ion essential for activity. MshB isolated on the Ni-affinity column contains 0.36 equivalent of Ca and 0.82 equivalent of Ni, and less than 0.08 equivalent of Zn per subunit. MshB isolated on the Zn-affinity column contains less than 0.1 equivalent of Ca and 2.3 equivalents of Zn, and less than 0.08 equivalent of Ni per subunit. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity, but Ca2+ and Mg2+ produce no restoration of activity
Ni2+
-
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+
Zn2+
metal-dependent enzyme
Zn2+
contains an active site divalent transition metal. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity
Zn2+
metalloprotein, the deacetylase activity is completely dependent on the presence of a divalent metal cation. The Zn2+ is 5 coordinate with 3 residues from MshB (His-13, Asp-16, His-147) and two water molecules
Zn2+
MshB contains a divalent transition metal ion essential for activity. MshB isolated on the Ni-affinity column contains 0.36 equivalent of Ca and 0.82 equivalent of Ni, and less than 0.08 equivalent of Zn per subunit. MshB isolated on the Zn-affinity column contains less than 0.1 equivalent of Ca and 2.3 equivalents of Zn, and less than 0.08 equivalent of Ni per subunit. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity, but Ca2+ and Mg2+ produce no restoration of activity
Zn2+
MshB is a Zn2+ metalloprotein, the deacetylase activity is completely dependent on the presence of a divalent metal cation. The Zn2+ is 5 coordinate with 3 residues from MshB (His-13, Asp-16, His-147) and two water molecules
Zn2+
a zinc-dependent enzyme, binding structure of the catalytic zinc, overview
Zn2+
the active site metal ion is coordinated to two histidine residues, His13 and His147, and an aspartate, Asp16
Zn2+
zinc-metalloenzyme, the bound zinc ion is coordinated in the active site by His13, His147, and Asp16, and two water molecules
Zn2+
-
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+
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1,10-phenanthroline
0.1 mM, 82% inhibition of the enzyme isolated on the Ni-affinity column. 0.1mM 1,10-phenanthroline produces no signifiant inhibition of the enzyme isolated on the Zn-affinity column and 10% activity remains after treatment with 1 mM 1,10-phenanthroline. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity, but Ca2+ and Mg2+ produce no restoration of activity; inhibition of the Zn enzyme by 1,10-phenanthroline is slower or less complete than inhibition of the Ni enzyme. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity
benzyl 2-deoxy-2-acetamido-1-thio-beta-D-glucopyranoside
-
0.5 mM, 13% inhibition
cyclohexyl (2''R),(2''S)-3,3''-anhydro-2-deoxy-2-C-(2'',3''-dihydroxypropyl)-alpha-D-glucopyranoside
-
0.5 mM, 6.6% inhibition
cyclohexyl 2-deoxy-2-C-(2'',3''-epoxypropyl)-alpha-D-glucopyranoside
-
0.5 mM, 19.7% inhibition
cyclohexyl 2-deoxy-2-C-(2''-hydroxypropyl)-alpha-D-glucopyranoside
-
0.5 mM, 11.4% inhibition
cyclohexyl 2-deoxy-2-C-(2''-oxopropyl)-a-D-glucopyranoside
-
0.5 mM, 6.7% inhibition
cyclohexyl-2-chloroacetamido-2-deoxy-1-thio-alpha-D-glucopyranoside
-
0.5 mM, 15% inhibition
NaF
-
uncompetitive inhibitor, consistent with a metal-water/hydroxide functioning as the reactive nucleophile in the catalytic mechanism
phenyl-2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside
-
0.5 mM, 6% inhibition
phenyl-2-deoxy-2-acetamido-1-thio-beta-D-glucopyranoside
-
0.5 mM, 15% inhibition
phenyl-2-deoxy-2-[3'-(8''-hydroxy-3''-methyl-1'',4''-dioxo-1'',4''-dihydronaphthalen-2''-yl)butanamido]-1-thio-alpha-D-glucopyranoside
-
0.5 mM, 81.6% inhibition
phenyl-2-deoxy-2-[3'-(8''-hydroxy-3''-methyl-1'',4''-dioxo-1'',4''-dihydronaphthalen-2''-yl)pentanamido]-1-thio-alpha-D-glucopyranoside
-
0.5 mM, 81.4% inhibition
phenyl-2-deoxy-2-[3'-(8''-hydroxy-3''-methyl-1'',4''-dioxo-1'',4''-dihydronaphthalen-2''-yl)propanamido]-1-thio-alpha-D-glucopyranoside
-
0.5 mM, 57.4% inhibition
additional information
no inhibition is observed with 0.1 M 1,7-phenanthroline
-
additional information
-
no inhibition is observed with 0.1 M 1,7-phenanthroline
-
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0.34 - 0.348
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
0.34
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
pH 7.5, 30°C
9 - 400
N-acetyl-D-glucosamine
0.34
N-deacetyl-N-formylmycothiol-monobromobimane conjugate
pH 7.4, 37°C
1.695
phenyl-2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside
-
-
0.34
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
pH 7.5, 37°C
0.348
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
-
pH 7.5, 37°C
9
N-acetyl-D-glucosamine
-
mutant Y142F, pH 7.5, 30°C
17
N-acetyl-D-glucosamine
-
mutant Y142Q, pH 7.5, 30°C
17.5
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme E47A
22
N-acetyl-D-glucosamine
-
mutant Y142A, pH 7.5, 30°C
27
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme F216A
31
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme L19A
34
N-acetyl-D-glucosamine
-
Co2+-enzyme, pH 7.5, 30°C
36
N-acetyl-D-glucosamine
-
apo-enzyme, pH 7.5, 30°C
38
N-acetyl-D-glucosamine
pH 7.5, 30°C, wild-type enzyme
38
N-acetyl-D-glucosamine
-
wild-type, pH 7.5, 30°C
41
N-acetyl-D-glucosamine
-
Fe2+-enzyme, pH 7.5, 30°C
52
N-acetyl-D-glucosamine
-
mutant D15A, pH 7.5, 30°C
52
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme D15A
53
N-acetyl-D-glucosamine
-
Ni2+-enzyme, pH 7.5, 30°C
54
N-acetyl-D-glucosamine
-
Mn2+-enzyme, pH 7.5, 30°C
56
N-acetyl-D-glucosamine
-
Fe3+-enzyme, pH 7.5, 30°C
57
N-acetyl-D-glucosamine
-
mutant H144A, pH 7.5, 30°C
63
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme D146N
114
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme M98A
400
N-acetyl-D-glucosamine
-
above 400 mM, mutant D146A, pH 7.5, 30°C
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0.24 - 0.49
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
0.0048 - 2.1
N-acetyl-D-glucosamine
0.49
N-deacetyl-N-formylmycothiol-monobromobimane conjugate
pH 7.4, 37°C
0.12
phenyl-2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside
-
pH 7.5, 37°C
0.24
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
-
pH 7.5, 37°C
0.49
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
pH 7.5, 37°C
0.0048
N-acetyl-D-glucosamine
-
mutant D15A, pH 7.5, 30°C
0.0048
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme D15A
0.0095
N-acetyl-D-glucosamine
-
mutant Y142F, pH 7.5, 30°C
0.0115
N-acetyl-D-glucosamine
-
mutant H144A, pH 7.5, 30°C
0.02
N-acetyl-D-glucosamine
-
mutant Y142Q, pH 7.5, 30°C
0.03
N-acetyl-D-glucosamine
-
mutant Y142A, pH 7.5, 30°C
0.0333
N-acetyl-D-glucosamine
-
mutant D146A, pH 7.5, 30°C
0.047
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme D146N
0.11
N-acetyl-D-glucosamine
-
Fe3+-enzyme, pH 7.5, 30°C
0.13
N-acetyl-D-glucosamine
-
apo-enzyme, pH 7.5, 30°C
0.27
N-acetyl-D-glucosamine
-
Ni2+-enzyme, pH 7.5, 30°C
0.33
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme M98A
0.38
N-acetyl-D-glucosamine
-
Mn2+-enzyme, pH 7.5, 30°C
0.6
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme F216A
0.72
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme L19A
0.77
N-acetyl-D-glucosamine
pH 7.5, 30°C, wild-type enzyme
0.77
N-acetyl-D-glucosamine
-
wild-type, pH 7.5, 30°C
1.05
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme E47A
1.1
N-acetyl-D-glucosamine
-
Co2+-enzyme, pH 7.5, 30°C
2.1
N-acetyl-D-glucosamine
-
Fe2+-enzyme, pH 7.5, 30°C
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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
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
D146A
inactive mutant enzyme
D146A
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
D146A
-
inactive mutant enzyme
-
D146A
-
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
-
additional information
the enzyme is unable to catalyze the turnover of GlcNAc upon loss of the Arg68 or Asp95 side chains, consistent with the proposal that these side chains make critical hydrogen bonding interactions with substrate
additional information
-
the enzyme is unable to catalyze the turnover of GlcNAc upon loss of the Arg68 or Asp95 side chains, consistent with the proposal that these side chains make critical hydrogen bonding interactions with substrate
-
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Hayward, D.; Wiid, I.; van Helden, P.
Differential expression of mycothiol pathway genes: are they affected by antituberculosis drugs?
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Crystallization and preliminary X-ray analysis of N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis
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2003
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
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Nicholas, G.M.; Eckman, L.L.; Kovac, P.; Otero-Quintero, S.; Bewley, C.A.
Synthesis of 1-D- and 1-L-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside establishes substrate specificity of the Mycobacterium tuberculosis enzyme AcGI deacetylase
Bioorg. Med. Chem.
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2641-2647
2003
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
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Gammon, D.W.; Steenkamp, D.J.; Mavumengwana, V.; Marakalala, M.J.; Mudzunga, T.T.; Hunter, R.; Munyololo, M.
Conjugates of plumbagin and phenyl-2-amino-1-thioglucoside inhibit MshB, a deacetylase involved in the biosynthesis of mycothiol
Bioorg. Med. Chem.
18
2501-2514
2010
Mycobacterium tuberculosis
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Newton, G.L.; Av-Gay, Y.; Fahey, R.C.
N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis
J. Bacteriol.
182
6958-6963
2000
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
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The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold
J. Biol. Chem.
278
47166-47170
2003
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
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McCarthy, A.A.; Peterson, N.A.; Knijff, R.; Baker, E.N.
Crystallization and preliminary X-ray analysis of N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis
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335
1131-1141
2004
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis H37Rv (P9WJN3)
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Rawat, M.; Kovacevic, S.; Billman-Jacobe, H.; Av-Gay, Y.
Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis
Microbiology
149
1341-1349
2003
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis (A0R2I7), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0R2I7)
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Newton, G.L.; Ko, M.; Ta, P.; Av-Gay, Y.; Fahey, R.C.
Purification and characterization of Mycobacterium tuberculosis 1D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme
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47
542-550
2006
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
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Huang, X.; Hernick, M.
A fluorescence-based assay for measuring N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase activity
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414
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2011
Mycolicibacterium smegmatis
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The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) change depending on environmental conditions
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286
20275-20282
2011
Mycolicibacterium smegmatis
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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
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287
10424-10434
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A new crystal form of MshB from Mycobacterium tuberculosis with glycerol and acetate in the active site suggests the catalytic mechanism
Acta Crystallogr. Sect. D
68
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2012
Mycobacterium tuberculosis (P9WJN3)
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Huang, X.; Hernick, M.
Automated docking studies provide insights into molecular determinants of ligand recognition by N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB)
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Mycobacterium tuberculosis (P9WJN3)
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An enzyme-initiated Smiles rearrangement enables the development of an assay of MshB, the GlcNAc-Ins deacetylase of mycothiol biosynthesis
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Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis
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Molecular determinants of N-acetylglucosamine recognition and turnover by N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB)
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3784-3790
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Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis ATCC 25618 (P9WJN3)
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