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Information on EC 3.5.1.103 - N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
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EC Tree
3.5.1.103 N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylaseIUBMB Comments
This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway . In addition to acetylase activity, the enzyme possesses weak activity of EC 3.5.1.115, mycothiol S-conjugate amidase, and shares sequence similarity with that enzyme . The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+ .
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Word Map
- 3.5.1.103
- mycothiol
- mycobacterium
- tuberculosis
- amidase
- actinomycetes
-
s-conjugate
-
deacetylation
-
mycothiol-dependent
- isoniazid
-
electrophilic
-
low-molecular-weight
- smegmatis
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glcn-ins
-
alpha-helices
-
antituberculosis
- drug development
- medicine
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
rv1170, glcnac-ins deacetylase, acgi deacetylase, n-acetyl-1-d-myo-inosityl-2-amino-2-deoxy-alpha-d-glucopyranoside deacetylase, 1-d-myo-inosityl 2-n-acetamido-2-deoxy-alpha-d-glucopyranoside deacetylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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AcGI 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
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N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase
Rv1170
1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
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1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
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1-D-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
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1-D-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
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MshB
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MshB
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N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
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N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
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N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
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N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase
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N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)-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
proposed catalytic mechanism: the substrate binds to MshB so that the carbonyl oxygen of the acetyl group replaces the second water molecule on the Zn2+ ion. This leaves the first water molecule in an ideal position for general base-assisted nucleophilic attack of the carbonyl carbon of the acetyl group. The general base is the carboxylate of Asp-15. The tetrahedral transition state would then have a negatively charged oxygen atom that is stabilized by the positively charged Zn2+ and by the imidazolium side chain of His-144. Proton transfer to the nitrogen of the leaving group (GlcN-Ins) would be via the general acid function of the carboxyl group of Asp-15
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
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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
proposed catalytic mechanism of MshB, overview. MshB uses a general acid-base mechanism in which Asp15 and His144 act as the general base and acid catalysts respectively, while Tyr142 plays a dynamic role that includes stabilization of the oxyanion intermediate
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
proposed catalytic mechanism: the substrate binds to MshB so that the carbonyl oxygen of the acetyl group replaces the second water molecule on the Zn2+ ion. This leaves the first water molecule in an ideal position for general base-assisted nucleophilic attack of the carbonyl carbon of the acetyl group. The general base is the carboxylate of Asp-15. The tetrahedral transition state would then have a negatively charged oxygen atom that is stabilized by the positively charged Zn2+ and by the imidazolium side chain of His-144. Proton transfer to the nitrogen of the leaving group (GlcN-Ins) would be via the general acid function of the carboxyl group of Asp-15
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase
This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway [1]. In addition to acetylase activity, the enzyme possesses weak activity of EC 3.5.1.115, mycothiol S-conjugate amidase, and shares sequence similarity with that enzyme [2]. The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+ [3].
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CAS REGISTRY NUMBER
COMMENTARY
340703-87-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
-
?
cyclohexyl-2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside + H2O
cyclohexyl-2-amino-2-deoxy-1-thio-alpha-D-glucopyranoside + acetate
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6% of the activity with 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
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?
cyclohexyl-2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O
cyclohexyl-2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
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6% of the activity with 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
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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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-
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?
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
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?
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
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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-
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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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-
-
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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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-
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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
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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
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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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-
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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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-
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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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-
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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
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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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-
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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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-
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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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Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
MshB activity as a control point regulating mycothiol production
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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-
-
?
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
biosynthesis of mycothiol
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
mycothiol biosynthesis
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
MshB activity as a control point regulating mycothiol production
-
-
?
additional information
?
-
MshB activity as a control point regulating mycothiol production
-
-
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
MshB activity as a control point regulating mycothiol production
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Mn2+
Ni2+
Zn2+
additional information
-
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
Fe2+
the active site metal ion is coordinated to two histidine residues, His13 and His147, and an aspartate, Asp16
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
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
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Association of mycothiol with protection of Mycobacterium tuberculosis from toxic oxidants and antibiotics.
Tuberculosis
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8.
Tuberculosis
Crystallization and preliminary X-ray analysis of N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis.
Tuberculosis
N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis.
Tuberculosis
Purification and characterization of Mycobacterium tuberculosis 1D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme.
Tuberculosis
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.
Tuberculosis
Synthesis of natural product-inspired inhibitors of Mycobacterium tuberculosis mycothiol-associated enzymes: the first inhibitors of GlcNAc-Ins deacetylase.
Tuberculosis
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.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
pH 7.5, 30°C
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
17.5
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme E47A
27
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme F216A
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
pH 7.5, 30°C, mutant enzyme D15A
0.047
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme D146N
0.33
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme M98A
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
1.05
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme E47A
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
phenyl-2-acetamido-2-deoxy-1-thio-alpha-D-glucopyranoside
-
pH 7.5, 37°C
0.68
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
-
pH 7.5, 37°C
1.44
1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
pH 7.5, 37°C
0.00009
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme D15A
0.00074
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme D146N
0.0029
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme M98A
0.022
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme F216A
0.023
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme L19A
0.06
N-acetyl-D-glucosamine
pH 7.5, 30°C, mutant enzyme E47A
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
-
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
additional information
malfunction
disruption of mshB in Mycobacterium smegmatis results in decreased production of mycothiol (510% of the parent strain mc2155) but does not abolish mycothiol synthesis completely. Complementation of the MshB2 mutants with the mshB gene results in increased mycothiol production towards the exponential and stationary phases of the bacterial growth cycle. The results suggest that another enzyme is capable of mycothiol biosynthesis by providing N-acetylglucosaminylinositol deacetylation activity in the absence of MshB
malfunction
GlcNAc-Ins is absent in mycothiol-deficient mutant strain 49. This strain can concentrate GlcNAc-Ins from the medium and convert it to mycothiol
malfunction
-
GlcNAc-Ins is absent in mycothiol-deficient mutant strain 49. This strain can concentrate GlcNAc-Ins from the medium and convert it to mycothiol
-
metabolism
the enzyme is involved in the biosynthesis of mycothiol (MSH), a protective low molecular weight thiol present only in Mycobacterium tuberculosis and other actinomycetes
metabolism
the zinc-based deacetylase catalyses a step in the mycothiol biosynthetic pathway that involves the deacetylation of 1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol via cleavage of an amide bond, to 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol and acetate
metabolism
the zinc-based deacetylase catalyzes the fourth step in mycothiol biosynthesis, the deacetylation of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside to form 1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside and acetate
metabolism
Actinobacteria use the unique thiol mycothiol (MSH) as their primary reducing agent and in the detoxification of xenobiotics. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) is the metal-dependent deacetylase that catalyzes the deacetylation of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside, the committed step in MSH biosynthesis
metabolism
-
Actinobacteria use the unique thiol mycothiol (MSH) as their primary reducing agent and in the detoxification of xenobiotics. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) is the metal-dependent deacetylase that catalyzes the deacetylation of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside, the committed step in MSH biosynthesis
-
additional information
configuration strongly suggests that Asp15 acts both as a general base catalyst in the nucleophilic attack of water on the amide carbonyl C atom and in its protonated form acts as a general acid to protonate the amide N atom. Residue Tyr142 is involved in a conformational change on substrate binding and contributes to the oxyanion hole that stabilizes the tetrahedral intermediate
additional information
the core structure of MshB contains two homologous domains comprised of two alpha-helices sandwiched by a five-stranded beta-sheet, three-dimensional structure of MshB, Zn-MshB, PDB ID 1Q74
Show AA Sequence and Transmembrane Helices (3608 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
158000
32000
33423
79000
158000
tetramer, the enzyme behaves as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, gel filtration
32000
2 * 32000, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, SDS-PAGE
32000
4 * 32000, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, SDS-PAGE
33423
2 * 33423, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, calculated from sequence
33423
4 * 33423, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, calculated from sequence
79000
dimer, the enzyme behaves as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
dimer
2 * 32000, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, SDS-PAGE
dimer
2 * 33423, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, calculated from sequence
dimer
-
2 * 32000, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, SDS-PAGE
-
dimer
-
2 * 33423, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, calculated from sequence
-
tetramer
4 * 32000, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, SDS-PAGE
tetramer
4 * 33423, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, calculated from sequence
tetramer
-
4 * 32000, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, SDS-PAGE
-
tetramer
-
4 * 33423, the enzyme appears to behave as a dimer at normal ionic strength but may associate to a tetramer at low ionic strength, calculated from sequence
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals prepared in the presence of beta-octylglucoside as a key additive, are suitable for high-resolution X-ray structural analysis. The crystals are orthorhombic, with unit-cell parameters a = 71.69, b = 83.74, c = 95.65 A, space group P2(1)2(1)2(1) and two molecules in the asymmetric unit. Collection of X-ray diffraction data to 1.9 A resolution
hanging-drop vapour-diffusion method, crystallized both in native and SeMet-substituted forms
purified recombinant enzyme, from 0.1 M sodium acetate, 0.2 M ammonium sulfate, 25% PEG 4000 pH 4.6, with glycerol and the reaction product acetate in the active site, X-ray diffraction structure determination and analysis at 1.94 A resolution, modelling
structure, determined at 1.9 A resolution by X-ray crystallography
the structure, determined at 1.9 A resolution by X-ray crystallography, reveals an alpha/beta fold in which helices pack against a seven-stranded mostly parallel beta-sheet
vapor-diffusion method with a mother liquor consisting of 15% polyethylene glycol 4000, 50 mm Tris-HCl (pH 8.0), 0.1 m Mg(NO3)2, 6% 1,6-hexanediol, and 10% ethylene glycol. A 1:2 ratio of protein solution (6 mg/ml) to mother liquor is mixed and left for vapor equilibration. Triclinic crystals form after approximately 1 week at room temperature
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
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)
-
additional information
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
-
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli both in native and SeMet-substituted forms
Rv1170 is cloned to contain a C-terminal His-6 tag to facilitate purifiation, expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
fluorescence-based assay for measuring N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase activity that does not require HPLC analysis and can be carried out in multiwell plates. The fluorescamine-based assay can be used to determine the steady-state parameters for the deacetylation of N-acetyl-glucosamine by MshB
drug development
enzyme MshB is a target for the discovery of drugs to treat tuberculosis
medicine
medicine
antisense oligonucleotides to GlcNAc-Ins deacetylase (Rv1170) mRNA affect mycobacterial growth. The enzyme is sensitive to free radical generating antituberculosis drugs and may be a useful targets for new drug development
medicine
-
antisense oligonucleotides to GlcNAc-Ins deacetylase (Rv1170) mRNA affect mycobacterial growth. The enzyme is sensitive to free radical generating antituberculosis drugs and may be a useful targets for new drug development
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hayward, D.; Wiid, I.; van Helden, P.
Differential expression of mycothiol pathway genes: are they affected by antituberculosis drugs?
IUBMB Life
56
131-138
2004
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
brenda
McCarthy, A.A.; Knijff, R.; Peterson, N.A.; 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
Acta Crystallogr. Sect. D
59
2316-2318
2003
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
brenda
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.
11
2641-2647
2003
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
brenda
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
brenda
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)
brenda
Maynes, J.T.; Garen, C.; Cherney, M.M.; Newton, G.; Arad, D.; Av-Gay, Y.; Fahey, R.C.; James, M.N.
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)
brenda
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
J. Mol. Biol.
335
1131-1141
2004
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis H37Rv (P9WJN3)
brenda
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)
brenda
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
Protein Expr. Purif.
47
542-550
2006
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJN3)
brenda
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
Anal. Biochem.
414
278-281
2011
Mycolicibacterium smegmatis
brenda
Huang, X.; Kocabas, E.; Hernick, M.
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
J. Biol. Chem.
286
20275-20282
2011
Mycolicibacterium smegmatis
brenda
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
J. Biol. Chem.
287
10424-10434
2012
Mycolicibacterium smegmatis
brenda
Broadley, S.G.; Gumbart, J.C.; Weber, B.W.; Marakalala, M.J.; Steenkamp, D.J.; Sewell, B.T.
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
1450-1459
2012
Mycobacterium tuberculosis (P9WJN3)
brenda
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)
Biopolymers
101
406-417
2014
Mycobacterium tuberculosis (P9WJN3)
brenda
Lamprecht, D.A.; Muneri, N.O.; Eastwood, H.; Naidoo, K.J.; Strauss, E.; Jardine, A.
An enzyme-initiated Smiles rearrangement enables the development of an assay of MshB, the GlcNAc-Ins deacetylase of mycothiol biosynthesis
Org. Biomol. Chem.
10
5278-5288
2012
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis
brenda
Huang, X.; Hernick, M.
Molecular determinants of N-acetylglucosamine recognition and turnover by N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB)
Biochemistry
54
3784-3790
2015
Mycobacterium tuberculosis (P9WJN3), Mycobacterium tuberculosis ATCC 25618 (P9WJN3)
brenda
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