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Literature summary for 4.2.1.169 extracted from

  • Teramura, M.; Harada, J.; Tamiaki, H.
    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 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a 3-vinyl bacteriochlorophyllide d + H2O Chlorobaculum tepidum
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a 3-(1-hydroxyethyl) bacteriochlorophyllide d
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additional information Chlorobaculum tepidum the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV ?
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Organism

Organism UniProt Comment Textmining
Chlorobaculum tepidum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a 3-vinyl bacteriochlorophyllide d + H2O
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Chlorobaculum tepidum a 3-(1-hydroxyethyl) bacteriochlorophyllide d
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?
additional information the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV Chlorobaculum tepidum ?
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?
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 ?
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zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d + H2O
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Chlorobaculum tepidum zinc (31R)-8-ethyl-12-methyl-bacteriopheophorbide d + zinc (31S)-8-ethyl-12-methyl-bacteriopheophorbide d
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?

Synonyms

Synonyms Comment Organism
BchV
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Chlorobaculum tepidum

Expression

Organism Comment Expression
Chlorobaculum tepidum the transcriptional level of bchV gene is upregulated under low light conditions up

General Information

General Information Comment Organism
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
metabolism enzyme involvement in the biosynthetic pathways of BChl c homologues and epimers, overview Chlorobaculum tepidum
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