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Literature summary for 4.2.1.165 extracted from
- In vitro enzymatic assays of photosynthetic bacterial 3-vinyl hydratases for bacteriochlorophyll biosyntheses (2018), Photosynth. Res., 135, 319-328 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) | Chloroflexus aurantiacus |
| gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) | Chlorobaculum tepidum |
| gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) | Chloracidobacterium thermophilum |
| gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) | Chlorobaculum limnaeum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases | Chlorobaculum tepidum |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required, substrate-bound | Chloroflexus aurantiacus |  |
| Zn2+ | required, substrate-bound | Chlorobaculum tepidum | |
| Zn2+ | required, substrate-bound | Chloracidobacterium thermophilum | |
| Zn2+ | required, substrate-bound | Chlorobaculum limnaeum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | Chloroflexus aurantiacus | - |
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | Chlorobaculum tepidum | - |
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | Chloracidobacterium thermophilum | - |
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | Chlorobaculum limnaeum | - |
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | - |
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| a 3-(1-hydroxyethyl) bacteriochlorophyllide d | Chlorobaculum limnaeum | when 3V-bacteriochlorophyllide a is used as a substrate, all enzyme homoluges are effective in in vitro hydration | a 3-vinyl bacteriochlorophyllide d + H2O | - |
? | |
| a 3-(1-hydroxyethyl) bacteriochlorophyllide d | Chloroflexus aurantiacus | when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration | a 3-vinyl bacteriochlorophyllide d + H2O | - |
? | |
| a 3-(1-hydroxyethyl) bacteriochlorophyllide d | Chloracidobacterium thermophilum | when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration | a 3-vinyl bacteriochlorophyllide d + H2O | - |
? | |
| chlorophyllide a + H2O | Chloroflexus aurantiacus | - |
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | Chlorobaculum tepidum | - |
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | Chloracidobacterium thermophilum | - |
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | Chlorobaculum limnaeum | - |
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | - |
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chloracidobacterium thermophilum | G2LJR9 | - |
- |
| Chlorobaculum limnaeum | A0A1D8D5T2 | the organism contains three active enzyme homologues, ClimR0003, ClimR0008, and ClimR0017 | - |
| Chlorobaculum tepidum | Q8KBL0 | - |
- |
| Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | Q8KBL0 | - |
- |
| Chloroflexus aurantiacus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 12-methylated 3-vinyl bacteriochlorophyllide d + H2O | the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d | Chlorobaculum tepidum | ? | - |
? | |
| 12-methylated 3-vinyl bacteriochlorophyllide d + H2O | the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d | Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | ? | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | - |
Chloroflexus aurantiacus | 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | - |
Chlorobaculum tepidum | 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | - |
Chloracidobacterium thermophilum | 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | - |
Chlorobaculum limnaeum | 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | - |
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 3-vinyl bacteriochlorophyllide d + H2O | reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview | Chlorobaculum tepidum | (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 3-vinyl bacteriochlorophyllide d + H2O | reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview | Chloroflexus aurantiacus | (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d | ? | ? | |
| 3-vinyl bacteriochlorophyllide d + H2O | reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview | Chloracidobacterium thermophilum | (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d | ? | ? | |
| 3-vinyl bacteriochlorophyllide d + H2O | reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview | Chlorobaculum limnaeum | (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d | ? | ? | |
| 3-vinyl bacteriochlorophyllide d + H2O | reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview | Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 8-methylated 3-vinyl bacteriochlorophyllide d + H2O | the enzyme forms Zn-R[P,E]bacteriopheophorbide d as a major product and Zn-S[P,E]bacteriopheophorbide d as a minor one | Chlorobaculum tepidum | ? | - |
? | |
| a 3-(1-hydroxyethyl) bacteriochlorophyllide d | when 3V-bacteriochlorophyllide a is used as a substrate, all enzyme homoluges are effective in in vitro hydration | Chlorobaculum limnaeum | a 3-vinyl bacteriochlorophyllide d + H2O | - |
? | |
| a 3-(1-hydroxyethyl) bacteriochlorophyllide d | when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration | Chloroflexus aurantiacus | a 3-vinyl bacteriochlorophyllide d + H2O | - |
? | |
| a 3-(1-hydroxyethyl) bacteriochlorophyllide d | when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration | Chloracidobacterium thermophilum | a 3-vinyl bacteriochlorophyllide d + H2O | - |
? | |
| chlorophyllide a + H2O | - |
Chloroflexus aurantiacus | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | - |
Chlorobaculum tepidum | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | - |
Chloracidobacterium thermophilum | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | - |
Chlorobaculum limnaeum | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| chlorophyllide a + H2O | - |
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| additional information | both BchF and BchV from Chlorobaculum tepidum catalyze in vitro hydration of the 3-vinyl group of Zn-3V-[E,M]bacteriopheophorbide d. The reaction of Zn-3V-[E,E]bacteriopheophorbide d, the 121-methylated derivative of Zn-3V-[E,M]bacteriopheophorbides d, shows two products assigned to a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d. The R-epimeric product is predominant. Zn-3V-[P,E]bacteriopheophorbide d, the homologue methylated at the 82-position of Zn-3V-[E,E]bacteriopheophorbide d as a substrate gives similar results to that of Zn-3V-[E,E]bacteriopheophorbide d. Both BchF and BchV hydrate Zn-3V-[P,E]bacteriopheophorbide d stereoselectively and produce Zn-R[P,E]bacteriopheophorbide d as a major product and Zn-S[P,E]bacteriopheophorbide d as a minor one. With one more 82-methylated pigment, Zn-3V-[I,E]bacteriopheophorbide d, both BchF and BchV hydrate the 3-vinyl group of the substrate. No activity of BchF or BchV with Zn-3V-[I,E]bacteriopheophorbide c, the 20-methylated derivative of Zn-3V-[I,E]bacteriopheophorbide d. BchF and BchV can recognize the Pi-conjugated system as their substrate and 17,18-dihydrogenation of porphyrin to chlorin Pi-system is necessary for the substrate of BchF- and BchV-hydration, BchF is active with chlorin and bacteriochlorin in the Pi-conjugate, while BchV is only active with chlorin in the Pi-conjugate, both do not use the porphyrin Pi-conjugate, overview | Chlorobaculum tepidum | ? | - |
? | |
| additional information | the enzyme BchF produces an approximately 9:1 mixture of 31R- and S-epimers of the product | Chloroflexus aurantiacus | ? | - |
? | |
| additional information | both BchF and BchV from Chlorobaculum tepidum catalyze in vitro hydration of the 3-vinyl group of Zn-3V-[E,M]bacteriopheophorbide d. The reaction of Zn-3V-[E,E]bacteriopheophorbide d, the 121-methylated derivative of Zn-3V-[E,M]bacteriopheophorbides d, shows two products assigned to a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d. The R-epimeric product is predominant. Zn-3V-[P,E]bacteriopheophorbide d, the homologue methylated at the 82-position of Zn-3V-[E,E]bacteriopheophorbide d as a substrate gives similar results to that of Zn-3V-[E,E]bacteriopheophorbide d. Both BchF and BchV hydrate Zn-3V-[P,E]bacteriopheophorbide d stereoselectively and produce Zn-R[P,E]bacteriopheophorbide d as a major product and Zn-S[P,E]bacteriopheophorbide d as a minor one. With one more 82-methylated pigment, Zn-3V-[I,E]bacteriopheophorbide d, both BchF and BchV hydrate the 3-vinyl group of the substrate. No activity of BchF or BchV with Zn-3V-[I,E]bacteriopheophorbide c, the 20-methylated derivative of Zn-3V-[I,E]bacteriopheophorbide d. BchF and BchV can recognize the Pi-conjugated system as their substrate and 17,18-dihydrogenation of porphyrin to chlorin Pi-system is necessary for the substrate of BchF- and BchV-hydration, BchF is active with chlorin and bacteriochlorin in the Pi-conjugate, while BchV is only active with chlorin in the Pi-conjugate, both do not use the porphyrin Pi-conjugate, overview | Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bacterial 3-vinyl hydratase | - |
Chloroflexus aurantiacus |
| bacterial 3-vinyl hydratase | - |
Chlorobaculum tepidum |
| bacterial 3-vinyl hydratase | - |
Chloracidobacterium thermophilum |
| bacterial 3-vinyl hydratase | - |
Chlorobaculum limnaeum |
| bchF | - |
Chloroflexus aurantiacus |
| bchF | - |
Chlorobaculum tepidum |
| bchF | - |
Chloracidobacterium thermophilum |
| cfxBchF | - |
Chloroflexus aurantiacus |
| ClimR0003 | - |
Chlorobaculum limnaeum |
| ClimR0008 | - |
Chlorobaculum limnaeum |
| ClimR0017 | - |
Chlorobaculum limnaeum |
| craBchF | - |
Chloracidobacterium thermophilum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
assay at | Chloroflexus aurantiacus |
| 35 | - |
assay at | Chlorobaculum tepidum |
| 35 | - |
assay at | Chloracidobacterium thermophilum |
| 35 | - |
assay at | Chlorobaculum limnaeum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
assay at | Chloroflexus aurantiacus |
| 7.8 | - |
assay at | Chlorobaculum tepidum |
| 7.8 | - |
assay at | Chloracidobacterium thermophilum |
| 7.8 | - |
assay at | Chlorobaculum limnaeum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases. In vivo experiments with bchF-deleted mutants show considerably lower levels of bacteriochlorophyll a than the wild-type strain | Chlorobaculum tepidum |
| physiological function | a chlorosome is a large and efficient light-harvesting antenna system found in some photosynthetic bacteria. This system comprises self-aggregates of bacteriochlorophyll (BChl) c, d, or e possessing a chiral 1-hydroxyethyl group at the 3-position, which plays a key role in the formation of the supramolecule. Biosynthesis of chlorosomal pigments involves stereoselective conversion of 3-vinyl group to 3-(1-hydroxyethyl) group facilitated by a 3-vinyl hydratase. This 3-vinyl hydration also occurs in BChl a biosynthesis, followed by oxidation that introduces an acetyl group at the 3-position catalyzed by 3-vinyl hydratases. Analysis of the biosynthetic pathway of bacteriochlorophyll a and other chlorosomal pigments considering the substrate specificity and stereoselectivity, and comparisons of by 3-vinyl hydratases derived from green sulfur bacteria, overview. Chloroflexus aurantiacus possesses a 2:1 mixture of R/S[E,M]BChls c | Chloroflexus aurantiacus |
| physiological function | a chlorosome is a large and efficient light-harvesting antenna system found in some photosynthetic bacteria. This system comprises self-aggregates of bacteriochlorophyll (BChl) c, d, or e possessing a chiral 1-hydroxyethyl group at the 3-position, which plays a key role in the formation of the supramolecule. Biosynthesis of chlorosomal pigments involves stereoselective conversion of 3-vinyl group to 3-(1-hydroxyethyl) group facilitated by a 3-vinyl hydratase. This 3-vinyl hydration also occurs in BChl a biosynthesis, followed by oxidation that introduces an acetyl group at the 3-position catalyzed by 3-vinyl hydratases. Analysis of the biosynthetic pathway of BChl a and other chlorosomal pigments considering the substrate specificity and stereoselectivity, and comparisons of by 3-vinyl hydratases derived from green sulfur bacteria, overview | Chloracidobacterium thermophilum |
| physiological function | a chlorosome is a large and efficient light-harvesting antenna system found in some photosynthetic bacteria. This system comprises self-aggregates of bacteriochlorophyll (BChl) c, d, or e possessing a chiral 1-hydroxyethyl group at the 3-position, which plays a key role in the formation of the supramolecule. Biosynthesis of chlorosomal pigments involves stereoselective conversion of 3-vinyl group to 3-(1-hydroxyethyl) group facilitated by a 3-vinyl hydratase. This 3-vinyl hydration also occurs in BChl a biosynthesis, followed by oxidation that introduces an acetyl group at the 3-position catalyzed by 3-vinyl hydratases. Analysis of the biosynthetic pathway of BChl a and other chlorosomal pigments considering the substrate specificity and stereoselectivity, and comparisons of by 3-vinyl hydratases derived from green sulfur bacteria, overview | Chlorobaculum limnaeum |
| physiological function | a chlorosome is a large and efficient light-harvesting antenna system found in some photosynthetic bacteria. This system comprises self-aggregates of bacteriochlorophyll (BChl) c, d, or e possessing a chiral 1-hydroxyethyl group at the 3-position, which plays a key role in the formation of the supramolecule. Biosynthesis of chlorosomal pigments involves stereoselective conversion of 3-vinyl group to 3-(1-hydroxyethyl) group facilitated by a 3-vinyl hydratase. This 3-vinyl hydration also occurs in BChl a biosynthesis, followed by oxidation that introduces an acetyl group at the 3-position catalyzed by 3-vinyl hydratases. Analysis of the biosynthetic pathway of BChl a and other chlorosomal pigments considering the substrate specificity and stereoselectivity, and comparisons of by 3-vinyl hydratases derived from green sulfur bacteria, overview. The green sulfur bacterium Chlorobaculum tepidum synthesizes three types of chlorophyllous pigments: Chl aPD (Chl a esterified with DELTA2,6-phytadienol), BChl a, and BChl c. The core part of chlorosomes in Chlorobaculum tepidum consists of self-aggregates of BChl c molecules, which are a mixture of 31R/S-epimers as well as a mixture of 82-and 121-methylated homologues. In the cells, the chiral 31-carbon of BChl c species possessing the 8-ethyl group, 8-ethyl-12-methyl-([E,M]), and 8,12-diethyl-([E,E])BChls c, exclusively shows R-stereochemistry. The single 82-methylated species, 8-propyl-12-ethyl-([P,E])bacteriochlorophyll c, is a 9:1 mixture of 31R- and 31S-epimers, and bacteriochlorophyll c species with one more 82-methylation, 8-isobutyl-12-ethyl-([I,E])bacteriochlorophyll c, predominantly produces a 31S-epimer. Both BchF and BchV can hydrate the 3-vinyl group of chlorophyllide a as a substrate of the hydratases in the bacteriochlorophyll a biosynthetic pathway. Both BchF and BchV play a role in bacteriochlorophyll a biosynthesis, but BchF has a lower substrate specificity to the precursors of bacteriochlorophyll a than BchV | Chlorobaculum tepidum |
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