Ligand dimethylseleniopropionate
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Basic Ligand Information
Molecular Structure

C7H14O2S
dimethylseleniopropionate
PNOZGYVTMQEAID-UHFFFAOYSA-N
3-(thiolan-1-ium-1-yl)propanoate, diethylsulfoniopropionate
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (3 results)
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3-(thiolan-1-ium-1-yl)propanoate = thiolane + acrylate
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diethylsulfoniopropionate = diethylsulfide + acrylate
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dimethylseleniopropionate = dimethylselenide + acrylate
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (9 results)
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1.58
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30°C, pH not specified in the publication
1.71
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30°C, pH not specified in the publication
1.83
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30°C, pH not specified in the publication
2.04
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30°C, pH not specified in the publication
2.22
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30°C, pH not specified in the publication
4.25
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30°C, pH not specified in the publication
11.9
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30°C, pH not specified in the publication
21.9
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30°C, pH not specified in the publication
31.2
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30°C, pH not specified in the publication
KM Value (9 results)
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4.2
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30°C, pH not specified in the publication
5.7
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30°C, pH not specified in the publication
8.2
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30°C, pH not specified in the publication
16.4
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30°C, pH not specified in the publication
18.7
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30°C, pH not specified in the publication
21.4
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30°C, pH not specified in the publication
31.4
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30°C, pH not specified in the publication
31.4
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30°C, pH not specified in the publication
102.6
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30°C, pH not specified in the publication
References & Links
Literature References (2)
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Comparison of selenium and sulfur volatilization by dimethylsulfoniopropionate lyase (DMSP) in two marine bacteria and estuarine sediments
1997
Ansede, J.H.; Yoch, D.C.
FEMS Microbiol. Ecol.
23
315-324
Chemical differentiation of three DMSP lyases from the marine Roseobacter group
2017
Burkhardt, I.; Lauterbach, L.; Brock, N.; Dickschat, J.
Org. Biomol. Chem.
15
4432-4439
Links to other databases for dimethylseleniopropionate