4.4.1.3: dimethylpropiothetin dethiomethylase
This is an abbreviated version!
For detailed information about dimethylpropiothetin dethiomethylase, go to the full flat file.
Word Map on EC 4.4.1.3
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4.4.1.3
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h2s
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dimethylsulfide
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phytoplankton
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lyases
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hypotaurine
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roseobacter
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o-acetylserine
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ruegeria
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d-cysteine
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cupin
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rhodobacteraceae
- 4.4.1.3
- h2s
- dimethylsulfide
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phytoplankton
- lyases
- hypotaurine
- roseobacter
- o-acetylserine
- ruegeria
- d-cysteine
-
cupin
- rhodobacteraceae
Reaction
Synonyms
DddL lyase, dddP, DddQ, DddW, Dddy, desulfhydrase, dethiomethylase, dimethylpropiothetin, dimethylsulfoniopropionate lyase, DLA, DMSP, DMSP lyase, DMSP-lyase, F963_02809, SAMN05660830_03106, SL1157_2466
ECTree
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Metals Ions
Metals Ions on EC 4.4.1.3 - dimethylpropiothetin dethiomethylase
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Ca2+
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
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
Iron
Manganese
the presence of Fe(II) or Mn(II) elicits an about 40fold increase in DddW lyase activity compared to the apo-enzyme
Mn2+
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
additional information
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none of the metals Co, Cu, Mn, Ni or Zn is detected at above background levels
isolated protein contains 0.5 Fe per subunit. The UV-visible spectrum exhibits a feature at 550 nm, consistent with a tyrosinate-Fe(III) ligand-to-metal charge transfer transition. Both the Fe(III) oxidized and Fe(II) reduced species are active
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