BRENDA - Enzyme Database

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

Teramura, M.; Harada, J.; Tamiaki, H.; Photosyn. Res. 130, 33-45 (2016)

Data extracted from this reference:

Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.2.1.165
membrane
-
Chlorobaculum tepidum
16020
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.165
Chlorobaculum tepidum
Q8KBL0
-
-
4.2.1.169
Chlorobaculum tepidum
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.165
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
748858
Chlorobaculum tepidum
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
?
4.2.1.165
chlorophyllide a + H2O
-
748858
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
748858
Chlorobaculum tepidum
?
-
-
-
-
4.2.1.169
a 3-vinyl bacteriochlorophyllide d + H2O
-
748858
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
748858
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
748858
Chlorobaculum tepidum
?
-
-
-
-
4.2.1.169
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d + H2O
-
748858
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide d
-
-
-
?
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.2.1.165
membrane
-
Chlorobaculum tepidum
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
?
-
-
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.165
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
748858
Chlorobaculum tepidum
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
?
4.2.1.165
chlorophyllide a + H2O
-
748858
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
748858
Chlorobaculum tepidum
?
-
-
-
-
4.2.1.169
a 3-vinyl bacteriochlorophyllide d + H2O
-
748858
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
748858
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
748858
Chlorobaculum tepidum
?
-
-
-
-
4.2.1.169
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d + H2O
-
748858
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide d
-
-
-
?
Expression
EC Number
Organism
Commentary
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
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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
Expression (protein specific)
EC Number
Organism
Commentary
Expression
4.2.1.169
Chlorobaculum tepidum
the transcriptional level of bchV gene is upregulated under low light conditions
up