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Literature summary for 1.3.1.84 extracted from

  • Reisch, C.; Crabb, W.; Gifford, S.; Teng, Q.; Stoudemayer, M.; Moran, M.; Whitman, W.
    Metabolism of dimethylsulphoniopropionate by Ruegeria pomeroyi DSS-3 (2013), Mol. Microbiol., 89, 774-791 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene SPO1914, the gene is adjacent to and predicted to be within the same transcriptional unit as dmdA, which encodes the enzyme for the first step of the demethylation pathway Ruegeria pomeroyi

Protein Variants

Protein Variants Comment Organism
additional information construction of a gene SPO1914 disruption mutant by homologous recombination of suicide plasmids, the mutant is unable to grow on acrylate as the sole carbon source Ruegeria pomeroyi

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-dependent oxidoreductase Ruegeria pomeroyi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acrylyl-CoA + NADPH + H+ Ruegeria pomeroyi
-
propanoyl-CoA + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Ruegeria pomeroyi Q5LS56
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme by anion exchange and hydrophobic interaction chromatography, ultrafiltration, hydroxyapatatite chromatography, and again ultrafiltration. The enzyme is separated from acryloyl-CoA hydratase Ruegeria pomeroyi

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:D-glucose-grown cell low enzyme activity Ruegeria pomeroyi
-
culture condition:dimethylsulphoniopropionate-grown cells high enzyme activity Ruegeria pomeroyi
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [Āµmol/min/mg] Specific Activity Maximum [Āµmol/min/mg] Comment Organism
0.016
-
enzyme activity in crude cell extract of D-glucose-grown cells, pH 7.5, temperature not specified in the publication Ruegeria pomeroyi
0.195
-
enzyme activity in crude cell extract of dimethylsulphoniopropionate-grown cells, pH 7.5, temperature not specified in the publication Ruegeria pomeroyi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acrylyl-CoA + NADPH + H+
-
Ruegeria pomeroyi propanoyl-CoA + NADP+
-
?
additional information the partially purified recombinant protein has activity of acryloyl-CoA reductase but not 3-hydroxypropionyl-CoA reductase. The 3-hydroxypropionyl-CoA reductase activity observed in cell extracts results from the coupling of the acryloyl-CoA hydratase with an acryloyl-CoA reductase activity Ruegeria pomeroyi ?
-
?

Synonyms

Synonyms Comment Organism
acrylyl-CoA reductase
-
Ruegeria pomeroyi
AcuI
-
Ruegeria pomeroyi
NADPH-dependent acryloyl-CoA reductase activity
-
Ruegeria pomeroyi
SPO1914
-
Ruegeria pomeroyi
SPO_1914
-
Ruegeria pomeroyi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Ruegeria pomeroyi

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Ruegeria pomeroyi

Expression

Organism Comment Expression
Ruegeria pomeroyi the enzyme is induced 14fold in dimethylsulphoniopropionate-grown cells up

General Information

General Information Comment Organism
malfunction a SPO1914 mutant is unable to grow on acrylate as the sole carbon source, supporting its role in the dimethylsulphoniopropionate assimilation pathway Ruegeria pomeroyi
metabolism Ruegeria pomeroyi DSS-3 possesses two general pathways for metabolism of dimethylsulphoniopropionate (DMSP), an osmolyte of algae and abundant carbon source for marine bacteria. In the DMSP cleavage pathway, acrylate is transformed into acryloyl-CoA by propionate-CoA ligase (SPO2934) and other unidentified acyl-CoA ligases. Acryloyl-CoA is then reduced to propionyl-CoA by AcuI or SPO1914. Acryloyl-CoA is also rapidly hydrated to 3-hydroxypropionyl-CoA by acryloyl-CoA hydratase (SPO0147) Ruegeria pomeroyi