Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Pseudomonas stutzeri |
Crystallization (Comment) | Organism |
---|---|
mutant D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D, to 2.3 A resolution. The TS-PTDH monomer may be divided into a large and a small domain, separated by a flexible hinge region. The NAD+ cofactor is housed at the junction between the two domains, where residues from the large subunit engage in interactions with the ligand. In the cocrystal structure with NAD+ and inhibitor sulfite, the sulfite anion is situated proximal to the nicotinamide of the cofactor, where it is engaged through interactions with the side chains of Arg237, His292, and the backbone amides of Lys76 and Gly77 | Pseudomonas stutzeri |
Protein Variants | Comment | Organism |
---|---|---|
D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D | thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity | Pseudomonas stutzeri |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
sulfite | competitive, cocrystal structure | Pseudomonas stutzeri |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas stutzeri | O69054 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
PTDH | - |
Pseudomonas stutzeri |