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 | 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 | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | zinc-dependent oxidoreductase | Ruegeria pomeroyi |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acrylyl-CoA + NADPH + H+ | Ruegeria pomeroyi | - |
propanoyl-CoA + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ruegeria pomeroyi | Q5LS56 | - |
- |
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 | 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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/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 | 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 | 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Ruegeria pomeroyi |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Ruegeria pomeroyi |
Organism | Comment | Expression |
---|---|---|
Ruegeria pomeroyi | the enzyme is induced 14fold in dimethylsulphoniopropionate-grown cells | up |
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 |