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Literature summary for 1.3.1.75 extracted from
- Rapid C8-vinyl reduction of divinyl-chlorophyllide a by BciA from Rhodobacter capsulatus (2018), J. Photochem. Photobiol. A, 353, 661-666 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli Rosetta2 cells | Rhodobacter capsulatus |
| gene bciA or RCAP_rcc03260, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally Strep II-tagged enzyme in Escherichia coli strain Rosetta 2 | Rhodobacter capsulatus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Lineweaver-Burk plots, For the assay using BciA prepared under the high-salt condition (1.0 M NaCl), the assay buffer is supplemented with 1.0 M NaCl | Rhodobacter capsulatus | |
| 0.023 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged oligomeric enzyme, low salt condition | Rhodobacter capsulatus |  |
| 0.023 | - |
3,8-divinyl protochlorophyllide a | oligomeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
| 0.032 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, low salt condition | Rhodobacter capsulatus | |
| 0.032 | - |
3,8-divinyl protochlorophyllide a | dimeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
| 0.035 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, high salt condition | Rhodobacter capsulatus | |
| 0.035 | - |
3,8-divinyl protochlorophyllide a | dimeric enzyme (high salt condition, 1 M NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
since the oligomeric BciA eluted from the Sephacryl S-200HR column is estimated to have a mass above 200 kDa, it is a hexamer or larger complex | Rhodobacter capsulatus |
| 200000 | - |
gel filtration | Rhodobacter capsulatus |
| 200000 | - |
above, recombinant N-terminally Strep II-tagged enzyme BciA, gel filtration | Rhodobacter capsulatus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3,8-divinyl chlorophyllide a + NADPH + H+ | Rhodobacter capsulatus | - |
chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl chlorophyllide a + NADPH + H+ | Rhodobacter capsulatus NBRC 16581 | - |
chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl chlorophyllide a + NADPH + H+ | Rhodobacter capsulatus ATCC BAA-309 | - |
chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl chlorophyllide a + NADPH + H+ | Rhodobacter capsulatus SB1003 | - |
chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | Rhodobacter capsulatus | - |
protochlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | Rhodobacter capsulatus NBRC 16581 | - |
protochlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | Rhodobacter capsulatus ATCC BAA-309 | - |
protochlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | Rhodobacter capsulatus SB1003 | - |
protochlorophyllide a + NADP+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodobacter capsulatus | - |
- |
- |
| Rhodobacter capsulatus | D5ARW2 | - |
- |
| Rhodobacter capsulatus ATCC BAA-309 | D5ARW2 | - |
- |
| Rhodobacter capsulatus NBRC 16581 | D5ARW2 | - |
- |
| Rhodobacter capsulatus SB1003 | - |
- |
- |
| Rhodobacter capsulatus SB1003 | D5ARW2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally Strep II-tagged enzyme from Escherichia coli strain Rosetta 2 by affinity chromatography and gel filtration | Rhodobacter capsulatus |
| Strep-Tactin Sepharose column chromatography and Sephacryl S-200 gel filtration | Rhodobacter capsulatus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3,8-divinyl chlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus | chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl chlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus NBRC 16581 | chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl chlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus ATCC BAA-309 | chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl chlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus SB1003 | chlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus | protochlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus NBRC 16581 | protochlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus ATCC BAA-309 | protochlorophyllide a + NADP+ | - |
? | |
| 3,8-divinyl protochlorophyllide a + NADPH + H+ | - |
Rhodobacter capsulatus SB1003 | protochlorophyllide a + NADP+ | - |
? | |
| additional information | measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction | Rhodobacter capsulatus | ? | - |
- |
|
| additional information | measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction | Rhodobacter capsulatus NBRC 16581 | ? | - |
- |
|
| additional information | measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction | Rhodobacter capsulatus ATCC BAA-309 | ? | - |
- |
|
| additional information | measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction | Rhodobacter capsulatus SB1003 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 35000, Strep-tag II-tagged enzyme, SDS-PAGE | Rhodobacter capsulatus |
| ? | x * 35900, Strep-tag II-tagged enzyme, calculated from amino acid sequence | Rhodobacter capsulatus |
| More | BciA forms a functional oligomeric complex consisting of at least three rigid dimers. BciA requires NADPH as an electron donor for its C8-vinyl reduction activity. The BciA oligomer shows 90fold higher kcat values compared to the dimer. On the other hand, the dimer shows the similar kcat values both on the high and low NaCl concentrations. These suggests that disassembly of the oligomer to the dimer induces a structural change around the catalytic site of the enzyme, thereby decreasing the enzymatic activity of the dimer. In contrast, the Km value for the oligomer is comparable to that for the dimer, suggesting that the affinity of BciA for the substrate DV-Chlide a is retained following disassembly of the oligomer to the dimer. The oligomerization of BciA does not cause any allosteric effect on binding of DV-Chlide a at the catalytic center | Rhodobacter capsulatus |
| oligomer | x * 35900, recombinant N-terminally Strep II-tagged enzyme BciA, SDS-PAGE | Rhodobacter capsulatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BciA | - |
Rhodobacter capsulatus |
| C8-vinyl reductase | - |
Rhodobacter capsulatus |
| NADPH-dependent divinyl reductase | - |
Rhodobacter capsulatus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Rhodobacter capsulatus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0071 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, low salt condition | Rhodobacter capsulatus | |
| 0.0071 | - |
3,8-divinyl protochlorophyllide a | dimeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
| 0.0074 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, high salt condition | Rhodobacter capsulatus | |
| 0.0074 | - |
3,8-divinyl protochlorophyllide a | dimeric enzyme (high salt condition, 1 M NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
| 0.66 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged oligomeric enzyme, low salt condition | Rhodobacter capsulatus | |
| 0.66 | - |
3,8-divinyl protochlorophyllide a | oligomeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Rhodobacter capsulatus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | dependent on | Rhodobacter capsulatus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | BciA (NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR, EC 1.3.7.15). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR from Rhodobacter capsulatus, BciA has a lower affinity for DV-Chlide a but a much higher specific activity | Rhodobacter capsulatus |
| physiological function | BciA is a plant-type NADPH-dependent divinyl reductase, it works for reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms | Rhodobacter capsulatus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.21 | - |
3,8-divinyl protochlorophyllide a | dimeric enzyme (high salt condition, 1 M NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
| 0.211 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, high salt condition | Rhodobacter capsulatus | |
| 0.22 | - |
3,8-divinyl protochlorophyllide a | dimeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
| 0.222 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, low salt condition | Rhodobacter capsulatus | |
| 28.7 | - |
3,8-divinyl chlorophyllide a | pH 8.0, 22°C, recombinant Strep II-tagged oligomeric enzyme, low salt condition | Rhodobacter capsulatus | |
| 29 | - |
3,8-divinyl protochlorophyllide a | oligomeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C | Rhodobacter capsulatus | |
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