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Literature summary for 4.4.1.3 extracted from

  • Brummett, A.; Schnicker, N.; Crider, A.; Todd, J.; Dey, M.
    Biochemical, kinetic, and spectroscopic characterization of Ruegeria pomeroyi DddW - A mononuclear iron-dependent DMSP lyase (2015), PLoS ONE, 10, e0127288 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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 [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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
dynamic light scattering Ruegeria pomeroyi
36000
-
gel filtration Ruegeria pomeroyi

Organism

Organism UniProt Comment Textmining
Ruegeria pomeroyi Q5LW89
-
-
Ruegeria pomeroyi DSM 15171 Q5LW89
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Ruegeria pomeroyi

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-dimethylsulfoniopropanoate
-
Ruegeria pomeroyi dimethylsulfide + acrylate
-
?
beta-dimethylsulfoniopropanoate
-
Ruegeria pomeroyi DSM 15171 dimethylsulfide + acrylate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 18000-22000, SDS-PAGE, 2 * 18000, calculated from sequence, His-tagged recombinant protein Ruegeria pomeroyi

Synonyms

Synonyms Comment Organism
DddW
-
Ruegeria pomeroyi

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Ruegeria pomeroyi

kcat/KM [mM/s]

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