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IUBMB Comments The enzyme is involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton. Isolated from the bacterium Ruegeria pomeroyi .
Synonyms
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DmdD
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MTA-CoA hydratase
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SPO3805
locus name
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3-(methylsulfanyl)acryloyl-CoA + 2 H2O = acetaldehyde + methanethiol + CoA + CO2
3-(methylsulfanyl)acryloyl-CoA + H2O = 3-hydroxy-3-(methylsulfanyl)propanoyl-CoA
3-hydroxy-3-(methylsulfanyl)propanoyl-CoA = 3-oxopropanoyl-CoA + methanethiol
3-oxopropanoate = acetaldehyde + CO2
3-oxopropanoyl-CoA + H2O = 3-oxopropanoate + CoA
3-(methylsulfanyl)acryloyl-CoA + 2 H2O = acetaldehyde + methanethiol + CoA + CO2
overall reaction
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3-(methylsulfanyl)acryloyl-CoA + 2 H2O = acetaldehyde + methanethiol + CoA + CO2
overall reaction
3-(methylsulfanyl)acryloyl-CoA + 2 H2O = acetaldehyde + methanethiol + CoA + CO2
overall reaction
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3-(methylsulfanyl)acryloyl-CoA + H2O = 3-hydroxy-3-(methylsulfanyl)propanoyl-CoA
(1a)
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3-(methylsulfanyl)acryloyl-CoA + H2O = 3-hydroxy-3-(methylsulfanyl)propanoyl-CoA
(1a)
3-(methylsulfanyl)acryloyl-CoA + H2O = 3-hydroxy-3-(methylsulfanyl)propanoyl-CoA
(1a)
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3-hydroxy-3-(methylsulfanyl)propanoyl-CoA = 3-oxopropanoyl-CoA + methanethiol
(1b)
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3-hydroxy-3-(methylsulfanyl)propanoyl-CoA = 3-oxopropanoyl-CoA + methanethiol
(1b)
3-hydroxy-3-(methylsulfanyl)propanoyl-CoA = 3-oxopropanoyl-CoA + methanethiol
(1b)
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3-oxopropanoate = acetaldehyde + CO2
(1d)
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3-oxopropanoate = acetaldehyde + CO2
(1d)
3-oxopropanoate = acetaldehyde + CO2
(1d)
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3-oxopropanoyl-CoA + H2O = 3-oxopropanoate + CoA
(1c)
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3-oxopropanoyl-CoA + H2O = 3-oxopropanoate + CoA
(1c)
3-oxopropanoyl-CoA + H2O = 3-oxopropanoate + CoA
(1c)
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3-(methylsulfanyl)prop-2-enoyl-CoA hydro-lyase (acetaldehyde-forming)
The enzyme is involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton. Isolated from the bacterium Ruegeria pomeroyi.
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3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: the enzyme involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton
?
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: 3-(methylthio)acryloyl-CoA i.e. 3-(methylthio)prop-2-enoyl-CoA. 3-Methylmercaptopropionate-CoA cannot be hydrated and is only hydrolyzed slowly by the enzyme. Replacement of the sulfur atom in 3-(methylthio)acryloyl-CoA with a methylene group abolishes hydrolysis
?
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: 3-(methylthio)acryloyl-CoA i.e. 3-(methylthio)prop-2-enoyl-CoA
?
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: the enzyme involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton
?
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: 3-(methylthio)acryloyl-CoA i.e. 3-(methylthio)prop-2-enoyl-CoA. 3-Methylmercaptopropionate-CoA cannot be hydrated and is only hydrolyzed slowly by the enzyme. Replacement of the sulfur atom in 3-(methylthio)acryloyl-CoA with a methylene group abolishes hydrolysis
?
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: the enzyme involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton
?
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: 3-(methylthio)acryloyl-CoA i.e. 3-(methylthio)prop-2-enoyl-CoA
?
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3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: the enzyme involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton
?
3-(methylthio)acryloyl-CoA + 2 H2O
acetaldehyde + methanethiol + CoA + CO2
Substrates: the enzyme involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton
?
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SwissProt
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SwissProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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malfunction
a dmdD (SPO3805::tet) mutant fails to grow with 3-methylmercaptopropionate, and growth on dimethylsulphoniopropionate is severely inhibited
malfunction
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a dmdD (SPO3805::tet) mutant fails to grow with 3-methylmercaptopropionate, and growth on dimethylsulphoniopropionate is severely inhibited
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metabolism
the enzyme is involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton. The transcript for dmdD increases during growth on methylmercaptopropionate or dimethylsulphoniopropionate
metabolism
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the enzyme is involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton. The transcript for dmdD increases during growth on methylmercaptopropionate or dimethylsulphoniopropionate
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DMDD_RUEPO
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
267
0
28836
Swiss-Prot
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hexamer
composed of a dimer of trimers where the three monomers of each trimer are related by a crystallographic 3-fold axis
hexamer
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composed of a dimer of trimers where the three monomers of each trimer are related by a crystallographic 3-fold axis
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crystals of the wild-type enzyme and the E121A mutant enzyme are grown at 20°C by the hanging-drop vapor diffusion method. Crystal structure of the free enzyme at 1.5 A resolution, structures of the E121A mutant in complex with methylthioacryloyl-CoA and 3-methylmercaptopropionate-CoA at 1.8 A resolution
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E121A
crystal structures of the E121A mutant in complex with methylthioacryloyl-CoA and 3-methylmercaptopropionate-CoA at 1.8 A resolution
E121A
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crystal structures of the E121A mutant in complex with methylthioacryloyl-CoA and 3-methylmercaptopropionate-CoA at 1.8 A resolution
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the recombinant protein, with a C-terminal hexahistidine tag, was over-expressed in E. coli BL21 (DE3) Star cells
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Reisch, C.R.; Stoudemayer, M.J.; Varaljay, V.A.; Amster, I.J.; Moran, M.A.; Whitman, W.B.
Novel pathway for assimilation of dimethylsulphoniopropionate widespread in marine bacteria
Nature
473
208-211
2011
Ruegeria pomeroyi (Q5LLW6), Ruegeria pomeroyi DSM 15171 (Q5LLW6)
brenda
Tan, D.; Crabb, W.M.; Whitman, W.B.; Tong, L.
Crystal structure of DmdD, a crotonase superfamily enzyme that catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA
PLoS One
8
e63870
2013
Ruegeria pomeroyi (Q5LLW6), Ruegeria pomeroyi DSM 15171 (Q5LLW6)
brenda
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