Literature summary extracted from
Giraud, M.F.; Leonard, G.A.; Field, R.A.; Berlind, C.; Naismith, J.H.
RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase (2000), Nat. Struct. Biol., 7, 398-402.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
5.1.3.13 |
the structure is determined by multiwavelength anomalous diffraction to a resolution of 2.17 A |
Salmonella enterica |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
5.1.3.13 |
additional information |
Salmonella enterica |
third enzyme of dTDP-L-rhamnose pathway |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.1.3.13 |
Salmonella enterica |
- |
serovar typhimurium |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.1.3.13 |
additional information |
third enzyme of dTDP-L-rhamnose pathway |
Salmonella enterica |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
5.1.3.13 |
dimer |
each monomer is formed mainly from two beta-sheets arranged in a beta-sandwich. The structure of a dTDP-phenol-enzyme complex shows the substrate-binding site to be located between the two beta-sheets, this site is formed from residues of both monomers |
Salmonella enterica |