3.5.1.103: N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
This is an abbreviated version!
For detailed information about N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase, go to the full flat file.
Word Map on EC 3.5.1.103
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3.5.1.103
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mycothiol
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mycobacterium
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tuberculosis
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amidase
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actinomycetes
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s-conjugate
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deacetylation
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mycothiol-dependent
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isoniazid
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electrophilic
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low-molecular-weight
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smegmatis
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glcn-ins
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alpha-helices
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antituberculosis
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drug development
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medicine
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analysis
- 3.5.1.103
- mycothiol
- mycobacterium
- tuberculosis
- amidase
- actinomycetes
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s-conjugate
-
deacetylation
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mycothiol-dependent
- isoniazid
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electrophilic
-
low-molecular-weight
- smegmatis
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glcn-ins
-
alpha-helices
-
antituberculosis
- drug development
- medicine
- analysis
Reaction
Synonyms
1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, 1-D-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, 1D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, AcGI deacetylase, GlcNAc-Ins deacetylase, GlcNAc-Ins-deacetylase, MshB, N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase, N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-D-glucopyranoside deacetylase, N-acetyl-1-D-myo-inosityl-2-deoxy-alpha-D-glucopyranoside deacetylase, N-acetylglucosaminylinositol-deacetylase, Rv1170
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General Information
General 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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malfunction
metabolism
additional information
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
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GlcNAc-Ins is absent in mycothiol-deficient mutant strain 49. This strain can concentrate GlcNAc-Ins from the medium and convert it to mycothiol
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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
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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
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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