EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.3.1.14 | purified L-RhI alone and in complexes with L-rhamnose and D-allose, X-ray diffraction structure determination and analysis at 1.97-2.0 A resolution | Pseudomonas stutzeri |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.1.14 | D-allose | Pseudomonas stutzeri | - |
D-psicose | - |
r | |
5.3.1.14 | L-Rhamnose | Pseudomonas stutzeri | - |
L-Rhamnulose | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.3.1.14 | Pseudomonas stutzeri | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.1.14 | D-allose | - |
Pseudomonas stutzeri | D-psicose | - |
r | |
5.3.1.14 | L-Rhamnose | - |
Pseudomonas stutzeri | L-Rhamnulose | - |
r | |
5.3.1.14 | additional information | substrate binding structue, overview, L-RhI can efficiently catalyze the isomerization between various aldoses and ketoses, showing a broad substrate specificity compared to L-RhI from Escherichia coli, relationship between structure and substrate specificity, overview, the beta1-alpha1 loop, Gly60ΒArg76, of L-RhI is involved in the substrate binding of a neighbouring molecule | Pseudomonas stutzeri | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.3.1.14 | tetramer | L-RhI has a large domain with a (beta/alpha)8 barrel fold and an additional small domain composed of seven alpha-helices, forming a homotetramer, crystal structure analysis | Pseudomonas stutzeri |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.3.1.14 | L-RhI | - |
Pseudomonas stutzeri |