EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.8.8 | gene acdB, DNA and amino acid sequence determination and analysis, genes acdA and acdB are arranged in a tandem, expression of gene acdB in Escherichia coli strain JM109 | Acinetobacter sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.3.8.8 | Ag+ | 1 mM, complete inhibition of the recombinant enzyme | Acinetobacter sp. | |
1.3.8.8 | Cu2+ | 1 mM, complete inhibition of the recombinant enzyme | Acinetobacter sp. | |
1.3.8.8 | Hg2+ | 1 mM, 61% inhibition of the recombinant enzyme | Acinetobacter sp. | |
1.3.8.8 | Mn2+ | 1 mM, 72% inhibition of the recombinant enzyme | Acinetobacter sp. | |
1.3.8.8 | Pb2+ | 1 mM, 23% inhibition of the recombinant enzyme | Acinetobacter sp. | |
1.3.8.8 | Zn2+ | 1 mM, 19% inhibition of the recombinant enzyme | Acinetobacter sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.3.8.8 | 0.068 | - |
lauroyl-CoA | pH 8.5, recombinant enzyme | Acinetobacter sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.3.8.8 | 64000 | - |
2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE | Acinetobacter sp. |
1.3.8.8 | 64833 | - |
2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE | Acinetobacter sp. |
1.3.8.8 | 135000 | - |
recombinant enzyme, gel filtration | Acinetobacter sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.8.8 | lauroyl-CoA + acceptor | Acinetobacter sp. | enzyme shows preference for long-chain fatty acids | 2-dodecenoyl-CoA + reduced acceptor | - |
? | |
1.3.8.8 | lauroyl-CoA + acceptor | Acinetobacter sp. M-1 | enzyme shows preference for long-chain fatty acids | 2-dodecenoyl-CoA + reduced acceptor | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.8.8 | Acinetobacter sp. | Q8L0X1 | gene acdB | - |
1.3.8.8 | Acinetobacter sp. M-1 | Q8L0X1 | gene acdB | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.3.8.8 | recombinant acdB-encoded enzyme from Escherichia coli | Acinetobacter sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.8.8 | lauroyl-CoA + acceptor | enzyme shows preference for long-chain fatty acids | Acinetobacter sp. | 2-dodecenoyl-CoA + reduced acceptor | - |
? | |
1.3.8.8 | lauroyl-CoA + acceptor | enzyme shows preference for long-chain fatty acids | Acinetobacter sp. M-1 | 2-dodecenoyl-CoA + reduced acceptor | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.3.8.8 | dimer | 2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE | Acinetobacter sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.8.8 | AcdB | - |
Acinetobacter sp. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.3.8.8 | 50 | - |
purified recombinant enzyme, 30 min, 80% remaining activity | Acinetobacter sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.3.8.8 | 8.5 | - |
- |
Acinetobacter sp. |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
1.3.8.8 | 8 | 10 | recombinant enzyme | Acinetobacter sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.8.8 | FAD | 1 mol per mol of subunit, participates directly in the catalytic reaction | Acinetobacter sp. |