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Literature summary extracted from
- Stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyll c by the hydratases BchF and BchV: adaptation of green sulfur bacteria to limited-light environments (2015), Mol. Microbiol., 98, 1184-1198.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.169 | gene bchF quantitative RT-PCR expression analysis, phylogenetic analysis | Chlorobaculum tepidum |
| 4.2.1.169 | gene bchV, quantitative RT-PCR expression analysis, phylogenetic analysis | Chlorobaculum tepidum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.2.1.169 | additional information | construction of gene bchV deletion mutants strain tepdF. A bchF and bchV double mutant is not viable, indicating that either bchF or bchV can partly substitute in the synthesis of BChl a | Chlorobaculum tepidum |
| 4.2.1.169 | additional information | construction of gene bchV deletion mutants strain tepdV. A bchF and bchV double mutant is not viable, indicating that either bchF or bchV can partly substitute in the synthesis of BChl a | Chlorobaculum tepidum |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.2.1.169 | chlorosome | - |
Chlorobaculum tepidum | 46858 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | Chlorobaculum tepidum | - |
a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? |  |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | Chlorobaculum tepidum | bacteriochlorophyllide d is converted to bacteriochlorophyllide c | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | Chlorobaculum tepidum WT2321 | bacteriochlorophyllide d is converted to bacteriochlorophyllide c | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | Chlorobaculum tepidum WT2321 | - |
a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | chlorophyllide a + H2O | Chlorobaculum tepidum | cf. EC 4.2.1.165 | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| 4.2.1.169 | chlorophyllide a + H2O | Chlorobaculum tepidum WT2321 | cf. EC 4.2.1.165 | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.165 | Chlorobaculum tepidum | - |
- |
- |
| 4.2.1.169 | Chlorobaculum tepidum | H2VFK0 | gene bchF | - |
| 4.2.1.169 | Chlorobaculum tepidum | Q8KBL0 | bchV | - |
| 4.2.1.169 | Chlorobaculum tepidum WT2321 | H2VFK0 | gene bchF | - |
| 4.2.1.169 | Chlorobaculum tepidum WT2321 | Q8KBL0 | bchV | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.165 | 3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O | - |
Chlorobaculum tepidum | (31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d | - |
? | |
| 4.2.1.165 | 3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O | - |
Chlorobaculum tepidum | (31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d | - |
? | |
| 4.2.1.165 | 3-vinyl-8-propyl-12-ethyl-bacteriochlorophyllide d + H2O | - |
Chlorobaculum tepidum | (31R)-(1-hydroxyethyl)-8-propyl-12-ethyl-bacteriochlorophyllide d | - |
? | |
| 4.2.1.165 | chlorophyllide a + H2O | - |
Chlorobaculum tepidum | (31R)-3-(1-hydroxyethyl)-chlorophyllide a | formation of R-enantiomer at the 1-hydroxyethyl group is predominantly synthesized | ? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide a + H2O | - |
Chlorobaculum tepidum | a 3-(1-hydroxyethyl) bacteriochlorophyllide a | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide a + H2O | enzyme BchV prefers the S-stereoisomer, stereospecific reaction | Chlorobaculum tepidum | a 3-(1-hydroxyethyl) bacteriochlorophyllide a | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide a + H2O | - |
Chlorobaculum tepidum WT2321 | a 3-(1-hydroxyethyl) bacteriochlorophyllide a | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide a + H2O | enzyme BchV prefers the S-stereoisomer, stereospecific reaction | Chlorobaculum tepidum WT2321 | a 3-(1-hydroxyethyl) bacteriochlorophyllide a | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | - |
Chlorobaculum tepidum | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | bacteriochlorophyllide d is converted to bacteriochlorophyllide c | Chlorobaculum tepidum | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | enzyme BchV prefers the S-stereoisomer, stereospecific reaction | Chlorobaculum tepidum | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | - |
Chlorobaculum tepidum WT2321 | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | bacteriochlorophyllide d is converted to bacteriochlorophyllide c | Chlorobaculum tepidum WT2321 | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | enzyme BchV prefers the S-stereoisomer, stereospecific reaction | Chlorobaculum tepidum WT2321 | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | chlorophyllide a + H2O | cf. EC 4.2.1.165 | Chlorobaculum tepidum | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| 4.2.1.169 | chlorophyllide a + H2O | cf. EC 4.2.1.165 | Chlorobaculum tepidum WT2321 | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.169 | bchF | - |
Chlorobaculum tepidum |
| 4.2.1.169 | BchV | - |
Chlorobaculum tepidum |
| 4.2.1.169 | C3-vinyl hydratase | - |
Chlorobaculum tepidum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.169 | 35 | - |
assay at | Chlorobaculum tepidum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.169 | 7.8 | - |
assay at | Chlorobaculum tepidum |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 4.2.1.169 | Chlorobaculum tepidum | transcriptional level of bchV is upregulated at lower light intensity, the Chlorobaculum tepidum adapts to low-light environments by control of the bchV transcription | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.165 | physiological function | deficiency in BchF impairs the production of both bacteriochlorophyllide a and bacteriochlorophyllide c.Pigment analyses of the BchF inactivated mutant, which still has BchV as a sole hydratase, shows higher ratios of S-epimeric bacteriochlorophyll c than the wild-type strain. The heightened prevalence of S-stereoisomers in the mutant is more remarkable at lower light intensities and causes a red shift of the chlorosomal Qy absorption band leading to advantages for light-energy transfer | Chlorobaculum tepidum |
| 4.2.1.169 | evolution | phylogenetic relationships of BchF and BchV orthologues, overview | Chlorobaculum tepidum |
| 4.2.1.169 | malfunction | BcF deficiency impairs the production of both bacteriochlorophylls BChl a and BChl c. The bchV-deletion mutant possessing only BchF shows a significant decrease of the S-epimers and accumulations of C3-vinyl BChl c species, while the bchF-inactivated mutant, which still has BchV as a sole hydratase, shows higher ratios of S-epimeric bacteriochlorophyll c than the wild-type strain. A bchF and bchV double mutant is not viable, indicating that either bchF or bchV can partly substitute in the synthesis of bacteriochlorophyl a | Chlorobaculum tepidum |
| 4.2.1.169 | malfunction | the bchV-deletion mutant possessing only BchF shows a significant decrease of the S-epimers and accumulations of C3-vinyl BChl c species, while the bchF-inactivated mutant, which still has BchV as a sole hydratase, shows higher ratios of S-epimeric bacteriochlorophyll c than the wild-type strain. The heightened prevalence of S-stereoisomers in the mutant is more remarkable at lower light intensities and causes a red shift of the chlorosomal Qy absorption band leading to advantages for light-energy transfer. A bchF and bchV double mutant is not viable, indicating that either bchF or bchV can partly substitute in the synthesis of bacteriochlorophyl a | Chlorobaculum tepidum |
| 4.2.1.169 | metabolism | in the absence of BchV, BchF catalyzes hydration of C3-vinyl groups for BChl c biosynthesis, predominantly to R-epimers, but has less activity for substrates with more methyl groups at the C81 position. The enzyme is also functional in the BChl a biosynthesis of Chlorobaculum tepidum | Chlorobaculum tepidum |
| 4.2.1.169 | metabolism | in the absence of BchV, BchF catalyzes hydration of C3-vinyl groups for BChl c biosynthesis, predominantly to R-epimers, but has less activity for substrates with more methyl groups at the C81 position. This enzyme is also functional in the BChl a biosynthesis of Chlorobaculum tepidum | Chlorobaculum tepidum |
| 4.2.1.169 | additional information | Chlorobaculum tepidum possess five enzymatically dependent homologs and epimers of bacteriochlorophyll c, R[E,M], R[E,E], R[P,E], S[P,E] and S[I,E]BChls c. The epimeric BChl homologues lead to different properties of self-aggregates in chlorosomes, and their composition is changed to growth conditions of green sulfur bacteria cells | Chlorobaculum tepidum |
| 4.2.1.169 | additional information | Chlorobaculum tepidum possess five enzymatically dependent homologues and epimers of bacteriochlorophyll c, R[E,M], R[E,E], R[P,E], S[P,E] and S[I,E]BChls c. The epimeric BChl homologues lead to different properties of self-aggregates in chlorosomes, and their composition is changed to growth conditions of green sulfur bacteria cells | Chlorobaculum tepidum |
| 4.2.1.169 | physiological function | BchF plays a significant role in BChl a synthesis, the enzyme is involved in the biosynthesis of bacteriochlorophylls a and d, it shows highest activity with chlorophyllide a and 3-vinyl bacteriochlorophyllide d, stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyllides a and d by the hydratases BchF and BchV, overview. In the absence of BchV, BchF catalyzes hydration of C3-vinyl groups for BChl c biosynthesis, predominantly to R-epimers, but has less activity for substrates with more methyl groups at the C81 position. The C3-1-hydroxyethyl group is essential for the formation of chlorosomal pigments with self-aggregation ability | Chlorobaculum tepidum |
| 4.2.1.169 | physiological function | the enzyme is involved in the biosynthesis of bacteriochlorophylls a and d, it shows highest activity with 3-vinyl bacteriochlorophyllide d, stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyllides a and d by the hydratases BchF and BchV, overview. BchV can perform the hydration step of BChl a biosynthesis although its catalytic activity may be lower than that of BchF. The C3-1-hydroxyethyl group is essential for the formation of chlorosomal pigments with self-aggregation ability. As transcriptional level of bchV is upregulated at lower light intensity, the Chlorobaculum tepidum adapts to low-light environments by control of the bchV transcription | Chlorobaculum tepidum |
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