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Literature summary extracted from
- In vitro stereospecific hydration activities of the 3-vinyl group of chlorophyll derivatives by BchF and BchV enzymes involved in bacteriochlorophyll c biosynthesis of green sulfur bacteria (2016), Photosynth. Res., 130, 33-45 .
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.2.1.165 | membrane | - |
Chlorobaculum tepidum | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.165 | 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | Chlorobaculum tepidum | - |
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? |  |
| 4.2.1.165 | chlorophyllide a + H2O | Chlorobaculum tepidum | - |
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | Chlorobaculum tepidum | - |
a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | additional information | Chlorobaculum tepidum | the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.165 | Chlorobaculum tepidum | Q8KBL0 | - |
- |
| 4.2.1.169 | Chlorobaculum tepidum | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.165 | 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O | - |
Chlorobaculum tepidum | 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a | - |
? | |
| 4.2.1.165 | chlorophyllide a + H2O | - |
Chlorobaculum tepidum | 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a | - |
? | |
| 4.2.1.165 | additional information | the secondary alcoholic hydroxy group is requisite for chlorosomal aggregation and biosynthesized by hydrating the 3-vinyl group of their precursors through chlorophyllide a 31-hydratase and 3-vinyl bacteriochlorophyllide d 31-hydratase. The enzyme catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c to the zinc (31R)-bacteriopheophorbide c homologue, with a slight amount of the (31S)-epimeric species. R-stereoselectivity is observed in the BchF-hydration of zinc 3-vinyl-8-ethyl-12-ethyl-bacteriopheophorbides c. The wild-type strain gives almost exclusively (31R)-epimers of 8-ethyl-12-methyl-(R[E,M]BChl c) and 8,12-diethyl-BChl c (R[E,E]BChl c), approximately 90% (31R)- and 10% (31S)-epimers of 8-propyl-12-ethyl-BChl c (R[P,E]BChl c and S[P,E]BChl c), and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c (S[I,E]BChl c), 4% 31S-epimers in the total amount of BChl c homologues | Chlorobaculum tepidum | ? | - |
? | |
| 4.2.1.169 | a 3-vinyl bacteriochlorophyllide d + H2O | - |
Chlorobaculum tepidum | a 3-(1-hydroxyethyl) bacteriochlorophyllide d | - |
? | |
| 4.2.1.169 | additional information | the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV | Chlorobaculum tepidum | ? | - |
? | |
| 4.2.1.169 | additional information | the enzyme catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d to the zinc 31R-bacteriopheophorbide d homologue with a slight amount of the 31S-epimric species. BchV-hydration of zinc 3-vinyl-8-ethyl and propyl-12-ethyl-bacteriopheophorbides c gives a relatively larger amount of the 31S-epimers. Stereoselectivity is observed in the BchF-hydration of zinc 3-vinyl-8-propyl-12-ethyl-bacteriopheophorbides c resulting in a relatively larger amount of the 31S-epimers | Chlorobaculum tepidum | ? | - |
? | |
| 4.2.1.169 | zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d + H2O | - |
Chlorobaculum tepidum | zinc (31R)-8-ethyl-12-methyl-bacteriopheophorbide d + zinc (31S)-8-ethyl-12-methyl-bacteriopheophorbide d | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.165 | 31-hydratase | - |
Chlorobaculum tepidum |
| 4.2.1.165 | bchF | - |
Chlorobaculum tepidum |
| 4.2.1.169 | BchV | - |
Chlorobaculum tepidum |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 4.2.1.169 | Chlorobaculum tepidum | the transcriptional level of bchV gene is upregulated under low light conditions | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.165 | malfunction | deletion of bchF gene affects the composition of 31R/S-epimers in composite BChls c: the bchF-deleted mutant has nearly 100% R-stereochemistry in [E,M]- and [E,E]BChl c, 9-12% S-stereochemistry in [P,E]BChl c, and nearly 100% S-stereochemistry in [I,E]BChl c | Chlorobaculum tepidum |
| 4.2.1.165 | metabolism | enzyme involvement in the biosynthetic pathways of BChl c homologues and epimers, overview | Chlorobaculum tepidum |
| 4.2.1.165 | physiological function | the photosynthetic green sulfur bacterium Chlorobaculum tepidum produces bacteriochlorophyll (BChl) c pigments bearing a chiral 1-hydroxyethyl group at the 3-position, which self-aggregate to construct main light-harvesting antenna complexes, chlorosomes. Chlorobaculum tepidum grown under a low limited light intensity increases the S-epimeric BChls c (6% of the total amount) and bathochromically shifts the red-most (Qy) absorption band of chlorosomal BChl c self-aggregates, which improves the efficiency of the excited energy transfer to an acceptor in chlorosomal envelopmental proteins. The enhancement of the S-epimers is explained by the fact that the transcriptional level of bchV gene is upregulated under low light conditions | Chlorobaculum tepidum |
| 4.2.1.169 | malfunction | deletion of bchV gene affects the composition of 31R/S-epimers in composite BChls c: the bchV-deleted mutant has nearly 100% R-stereochemistry in [E,M]- and [E,E]BChls c, 0-6% S-stereochemistry in [P,E]BChl c, and very few [I,E]BChl c | Chlorobaculum tepidum |
| 4.2.1.169 | metabolism | enzyme involvement in the biosynthetic pathways of BChl c homologues and epimers, overview | Chlorobaculum tepidum |
| 4.2.1.169 | physiological function | the photosynthetic green sulfur bacterium Chlorobaculum (Cba.) tepidum produces bacteriochlorophyll (BChl) c pigments bearing a chiral 1-hydroxyethyl group at the 3-position, which self-aggregate to construct main light-harvesting antenna complexes, chlorosomes. Chlorobaculum tepidum grown under a low limited light intensity increases the S-epimeric BChls c (6% of the total amount) and bathochromically shifts the red-most (Qy) absorption band of chlorosomal BChl c self-aggregates, which improves the efficiency of the excited energy transfer to an acceptor in chlorosomal envelopmental proteins. The enhancement of the S-epimers is explained by the fact that the transcriptional level of bchV gene is upregulated under low light conditions | Chlorobaculum tepidum |
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