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Literature summary for 1.1.1.396 extracted from
- Stereoselective C3-substituent modification and substrate channeling by oxidoreductase BchC in bacteriochlorophyll a biosynthesis (2019), FEBS Lett., 593, 799-809 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Rhodobacter capsulatus |
| expression in Escherichia coli | Chlorobaculum tepidum |
| gene bciC, recombinant expression of Strep II-tagged enzyme in Escherichia coli strain | Rhodobacter capsulatus |
| gene bciC, recombinant expression of Strep II-tagged enzyme in Escherichia coli strain | Chlorobaculum tepidum |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | BchC protein is a zinc-independent dehydrogenase | Chlorobaculum tepidum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | Rhodobacter capsulatus | - |
bacteriochlorophyllide a + NADH + H+ | - |
? |  |
| 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | Chlorobaculum tepidum | - |
bacteriochlorophyllide a + NADH + H+ | - |
? | |
| 31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | Rhodobacter capsulatus | - |
3-acetylchlorophyllide a + NADH + H+ | - |
? | |
| 31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | Chlorobaculum tepidum | - |
3-acetylchlorophyllide a + NADH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chlorobaculum tepidum | - |
- |
- |
| Chlorobaculum tepidum | Q93ST5 | - |
- |
| Rhodobacter capsulatus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Chlorobaculum tepidum |
| expression in Escherichia coli | Rhodobacter capsulatus |
| recombinant Strep II-tagged enzyme from Escherichia coli | Rhodobacter capsulatus |
| recombinant Strep II-tagged enzyme from Escherichia coli | Chlorobaculum tepidum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | - |
Rhodobacter capsulatus | bacteriochlorophyllide a + NADH + H+ | - |
r | |
| 3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | - |
Chlorobaculum tepidum | bacteriochlorophyllide a + NADH + H+ | - |
r | |
| 3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | - |
Rhodobacter capsulatus | 3-acetylchlorophyllide a + NADH + H+ | - |
r | |
| 3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | - |
Chlorobaculum tepidum | 3-acetylchlorophyllide a + NADH + H+ | - |
r | |
| 3-acetylchlorophyllide a + NADH + H+ | - |
Rhodobacter capsulatus | 3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | - |
r | |
| 3-acetylchlorophyllide a + NADH + H+ | - |
Chlorobaculum tepidum | 3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | - |
r | |
| 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | - |
Rhodobacter capsulatus | bacteriochlorophyllide a + NADH + H+ | - |
? | |
| 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | - |
Chlorobaculum tepidum | bacteriochlorophyllide a + NADH + H+ | - |
? | |
| 31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | - |
Rhodobacter capsulatus | 3-acetylchlorophyllide a + NADH + H+ | - |
? | |
| 31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+ | - |
Chlorobaculum tepidum | 3-acetylchlorophyllide a + NADH + H+ | - |
? | |
| bacteriochlorophyllide a + NADH + H+ | - |
Rhodobacter capsulatus | 3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | - |
r | |
| bacteriochlorophyllide a + NADH + H+ | - |
Chlorobaculum tepidum | 3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+ | - |
r | |
| additional information | BchC preferentially oxidizes 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. 31R-selectivity, overview. While most naturally occurring (B)Chls including BChl a have a magnesium ion at the center of the cyclic tetrapyrrole ring, zinc-chelated BChl a has been found in some organisms. BchC exhibits oxidation activity on zinc 3-(1-hydroxyethyl)-pheophorbide (Zn-3HE-Pheide) a, albeit at a low level, where the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The reduction of Zn-3Ac-Pheide a by BchC in the presence of NADH is also observed, predominantly producing the R-epimer of Zn-3HE-Pheide a. The chlorin pigments lacking a central metal, 3HE-Pheide a and 3Ac-Pheide a, are not suitable for substrates of BchC in the presence of NAD+ or NADH, respectively. Thus, the central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction. Determination of the 31-stereochemistry of 3HEChlide a and 3HE-BChlide a, overview | Chlorobaculum tepidum | ? | - |
- |
|
| additional information | BchC preferentially oxidizes 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. The enzyme catalyzes both the oxidation of 3HE to 3Ac and the reduction of 3Ac to 3HE, the reverse reaction. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. 31R-selectivity, overview. While most naturally occurring (B)Chls including BChl a have a magnesium ion at the center of the cyclic tetrapyrrole ring, zinc-chelated BChl a has been found in some organisms. BchC exhibits oxidation activity on zinc 3-(1-hydroxyethyl)-pheophorbide (Zn-3HE-Pheide) a, albeit at a low level, where the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The reduction of Zn-3Ac-Pheide a by BchC in the presence of NADH is also observed, predominantly producing the R-epimer of Zn-3HE-Pheide a. The chlorin pigments lacking a central metal, 3HE-Pheide a and 3Ac-Pheide a, are not suitable for substrates of BchC in the presence of NAD+ or NADH, respectively. Thus, the central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction. Determination of the 31-stereochemistry of 3HEChlide a and 3HE-BChlide a, overview | Rhodobacter capsulatus | ? | - |
- |
|
| zinc 3-(1-hydroxyethyl)-pheophorbide + NAD+ | the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The R-epimer is consumed as a substrate in the reverse reaction to a greater extent than is the S-epimer | Rhodobacter capsulatus | zinc 3-acetyl-(1-hydroxyethyl)-pheophorbide + NADH + H+ | - |
r | |
| zinc 3-(1-hydroxyethyl)-pheophorbide + NAD+ | the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The R-epimer is consumed as a substrate in the reverse reaction to a greater extent than is the S-epimer | Chlorobaculum tepidum | zinc 3-acetyl-(1-hydroxyethyl)-pheophorbide + NADH + H+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bchC | - |
Rhodobacter capsulatus |
| bchC | - |
Chlorobaculum tepidum |
| BchC oxidoreductase | - |
Rhodobacter capsulatus |
| BchC oxidoreductase | - |
Chlorobaculum tepidum |
| oxidoreductase BchC | - |
Rhodobacter capsulatus |
| oxidoreductase BchC | - |
Chlorobaculum tepidum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
assay at | Rhodobacter capsulatus |
| 35 | - |
assay at | Chlorobaculum tepidum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
assay at | Rhodobacter capsulatus |
| 7.8 | - |
assay at | Chlorobaculum tepidum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Rhodobacter capsulatus | |
| NAD+ | - |
Chlorobaculum tepidum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | BchC oxidoreductase is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis | Rhodobacter capsulatus |
| metabolism | BchC oxidoreductase is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis | Chlorobaculum tepidum |
| metabolism | the enzyme is involved in bacteriochlorophyll a biosynthesis | Rhodobacter capsulatus |
| metabolism | the enzyme is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis | Chlorobaculum tepidum |
| physiological function | BchC of Chlorobaculum tepidum preferentially oxidizes porphyrin-type pigments, 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a, in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. The enzyme catalyzes both the oxidation of 3HE to 3Ac and the reduction of 3Ac to 3HE, the reverse reaction. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. BchC of Rhodobacter capsulatus demonstrates the same 31R-selectivity, suggesting that utilization of 31R-epimers in BchC-catalyzed reductions may be conserved across different phyla of photosynthetic bacteria | Chlorobaculum tepidum |
| physiological function | BchC of Rhodobacter capsulatus preferentially oxidizes porphyrin-type pigments, 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a, in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. BchC of Chlorobaculum tepidum demonstrates the same 31R-selectivity, suggesting that utilization of 31R-epimers in BchC-catalyzed reductions may be conserved across different phyla of photosynthetic bacteria. The central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction | Rhodobacter capsulatus |
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