Application | Comment | Organism |
---|---|---|
drug development | enzyme MshB is a target for the discovery of drugs to treat tuberculosis | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | zinc-metalloenzyme, the bound zinc ion is coordinated in the active site by His13, His147, and Asp16, and two water molecules | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + H2O | Mycobacterium tuberculosis | - |
1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + acetate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WJN3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | 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 | Mycobacterium tuberculosis | ? | - |
? | |
N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + H2O | - |
Mycobacterium tuberculosis | 1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside + acetate | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
MshB | - |
Mycobacterium tuberculosis |
N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
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 | Mycobacterium tuberculosis |
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 | Mycobacterium tuberculosis |