Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli. Expression of recombinant DddW in minimal media in the absence of any added metal ion leads to the formation of insoluble protein | Ruegeria pomeroyi |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.5 | - |
beta-dimethylsulfoniopropanoate | presence of Mn2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi | |
8.68 | - |
beta-dimethylsulfoniopropanoate | presence of Fe2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cobalt | DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM | Ruegeria pomeroyi | |
copper | DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM | Ruegeria pomeroyi | |
Iron | the as-isolated enzyme contains 0.2-0.4 equivalents of bound iron. DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM, with Mn(II) and Fe(III) exhibiting weaker binding affinities. The presence of Fe(II) or Mn(II) elicits an about 40fold increase in DddW lyase activity compared to the apo-enzyme | Ruegeria pomeroyi | |
Manganese | the presence of Fe(II) or Mn(II) elicits an about 40fold increase in DddW lyase activity compared to the apo-enzyme | Ruegeria pomeroyi | |
Nickel | DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM | Ruegeria pomeroyi |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
dynamic light scattering | Ruegeria pomeroyi |
36000 | - |
gel filtration | Ruegeria pomeroyi |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ruegeria pomeroyi | Q5LW89 | - |
- |
Ruegeria pomeroyi DSM 15171 | Q5LW89 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant protein | Ruegeria pomeroyi |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.02 | - |
presence of Mn2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi |
1.08 | - |
presence of Fe2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-dimethylsulfoniopropanoate | - |
Ruegeria pomeroyi | dimethylsulfide + acrylate | - |
? | |
beta-dimethylsulfoniopropanoate | - |
Ruegeria pomeroyi DSM 15171 | dimethylsulfide + acrylate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 18000-22000, SDS-PAGE, 2 * 18000, calculated from sequence, His-tagged recombinant protein | Ruegeria pomeroyi |
Synonyms | Comment | Organism |
---|---|---|
DddW | - |
Ruegeria pomeroyi |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
17.33 | - |
beta-dimethylsulfoniopropanoate | presence of Mn2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi | |
18.25 | - |
beta-dimethylsulfoniopropanoate | presence of Fe2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Ruegeria pomeroyi |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.1 | - |
beta-dimethylsulfoniopropanoate | presence of Fe2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi | |
3.85 | - |
beta-dimethylsulfoniopropanoate | presence of Mn2+, pH 8.0, temperature not specified in the publication | Ruegeria pomeroyi |