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Literature summary for 1.3.1.75 extracted from
- A tale of two reductases extending the bacteriochlorophyll biosynthetic pathway in E. coli (2014), PLoS ONE, 9, e89734 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene bciA, recombinant expression in Escherichia coli strain BL21(DE3), coexpression with the enzymes of the biosynthetic pathway, engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli, overview. RSBciA is active, albeit not in vivo with the engineered pathway. Subcloning in Escherichia coli strain JM109 | Cereibacter sphaeroides |
| gene bciA, recombinant expression in Escherichia coli, coexpression with the enzymes of the biosynthetic pathway, engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli, overview. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway. Subcloning in Escherichia coli strain JM109 | Chlorobaculum tepidum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway. No mono-vinyl forms of any of the pathway intermediates upon coexpression of the 8-vinyl reductase with BchSID and BchM. PIX overproducing cells expressing BchSID and CTBciA alone produce two additional compounds, mono-vinyl PIX (mvPIX) and mono-vinyl MgPIX (mvMgPIX), indicating that CTBciA is capable of reducing the C8-vinyl group on both the Mg chelated and the non-Mg chelated porphyrin molecule | Chlorobaculum tepidum |
| additional information | engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. RSBciA is completely inactive in our recombinant system. RSBciA is completely inactive in our recombinant system. Subcloning in Escherichia coli strain JM109 | Cereibacter sphaeroides |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | Cereibacter sphaeroides | - |
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? |  |
| 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | Chlorobaculum tepidum | - |
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? | |
| 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | Chlorobaculum tepidum TLS | - |
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? | |
| 3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | Cereibacter sphaeroides | - |
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cereibacter sphaeroides | Q3IXP7 | - |
- |
| Chlorobaculum tepidum | Q8KDI7 | - |
- |
| Chlorobaculum tepidum TLS | Q8KDI7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Cereibacter sphaeroides |
| recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Chlorobaculum tepidum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | - |
Cereibacter sphaeroides | chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? | |
| 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | - |
Chlorobaculum tepidum | chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? | |
| 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | - |
Chlorobaculum tepidum TLS | chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? | |
| 3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ | - |
Cereibacter sphaeroides | protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster | - |
? | |
| additional information | the 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway | Chlorobaculum tepidum | ? | - |
? | |
| additional information | the native 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. Recombinant enzyme RSBciA is active, albeit not in vivo with the engineered pathway, but shows very slow activity | Cereibacter sphaeroides | ? | - |
? | |
| additional information | the 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway | Chlorobaculum tepidum TLS | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 8-vinyl reductase | - |
Cereibacter sphaeroides |
| 8-vinyl reductase | - |
Chlorobaculum tepidum |
| BciA | - |
Cereibacter sphaeroides |
| BciA | - |
Chlorobaculum tepidum |
| CTBciA | - |
Chlorobaculum tepidum |
| ct_1063 | - |
Chlorobaculum tepidum |
| NADPH-dependent reductase BciA | - |
Cereibacter sphaeroides |
| NADPH-dependent reductase BciA | - |
Chlorobaculum tepidum |
| RSBciA | - |
Cereibacter sphaeroides |
| RSP_3070 | - |
Cereibacter sphaeroides |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Cereibacter sphaeroides |
| 37 | - |
assay at | Chlorobaculum tepidum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Cereibacter sphaeroides |
| 8 | - |
assay at | Chlorobaculum tepidum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding | Cereibacter sphaeroides | |
| NADPH | NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding | Chlorobaculum tepidum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | green bacteria like Chlorobaculum tepidum are unique in that they are able to produce different types of Chls and Bchls, and encode in their genomes several homologs (BchS, T) of the large subunit (BchH) of the magnesium chelatase, which may play a role in regulating the types of (B)Chls produced | Chlorobaculum tepidum |
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Release 2023.1 (January 2023)
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