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
-
3.5.1.103
-
mycothiol
-
mycobacterium
-
tuberculosis
-
amidase
-
actinomycetes
-
s-conjugate
-
deacetylation
-
mycothiol-dependent
-
isoniazid
-
electrophilic
-
low-molecular-weight
-
smegmatis
-
glcn-ins
-
alpha-helices
-
antituberculosis
-
drug development
-
medicine
-
analysis
- 3.5.1.103
- mycothiol
- mycobacterium
- tuberculosis
- amidase
- actinomycetes
-
s-conjugate
-
deacetylation
-
mycothiol-dependent
- isoniazid
-
electrophilic
-
low-molecular-weight
- smegmatis
-
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
ECTree
Advanced search results
Metals Ions
Metals Ions on EC 3.5.1.103 - N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
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
the active site metal ion is coordinated to two histidine residues, His13 and His147, and an aspartate, Asp16
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
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