Literature summary extracted from
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 (2012), Acta Crystallogr. Sect. D, 68, 1450-1459.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.5.1.103 |
recombinant enzyme expression |
Mycobacterium tuberculosis |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.5.1.103 |
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 |
Mycobacterium tuberculosis |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.5.1.103 |
Zn2+ |
a zinc-dependent enzyme, binding structure of the catalytic zinc, overview |
Mycobacterium tuberculosis |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.5.1.103 |
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + H2O |
Mycobacterium tuberculosis |
- |
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + acetate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.1.103 |
Mycobacterium tuberculosis |
P9WJN3 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.5.1.103 |
recombinant enzyme |
Mycobacterium tuberculosis |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.5.1.103 |
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + H2O |
- |
Mycobacterium tuberculosis |
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + acetate |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.5.1.103 |
MshB |
- |
Mycobacterium tuberculosis |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.5.1.103 |
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 |
Mycobacterium tuberculosis |
3.5.1.103 |
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 |
Mycobacterium tuberculosis |