BRENDA - Enzyme Database

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

Harada, J.; Teramura, M.; Mizoguchi, T.; Tsukatani, Y.; Yamamoto, K.; Tamiaki, H.; Mol. Microbiol. 98, 1184-1198 (2015)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
4.2.1.169
gene bchF quantitative RT-PCR expression analysis, phylogenetic analysis; gene bchV, quantitative RT-PCR expression analysis, phylogenetic analysis
Chlorobaculum tepidum
Engineering
EC Number
Amino acid exchange
Commentary
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; 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
Commentary
Organism
GeneOntology No.
Textmining
4.2.1.169
chlorosome
;
Chlorobaculum tepidum
46858
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.165
3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
-
-
-
?
4.2.1.165
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
-
-
-
?
4.2.1.165
3-vinyl-8-propyl-12-ethyl-bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
(31R)-(1-hydroxyethyl)-8-propyl-12-ethyl-bacteriochlorophyllide d
-
-
-
?
4.2.1.165
chlorophyllide a + H2O
-
739109
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
-
739109
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
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
4.2.1.169
a 3-vinyl bacteriochlorophyllide a + H2O
-
739109
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
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
4.2.1.169
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
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
739109
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
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
4.2.1.169
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
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
739109
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
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
4.2.1.169
chlorophyllide a + H2O
cf. EC 4.2.1.165
739109
Chlorobaculum tepidum
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
4.2.1.169
chlorophyllide a + H2O
cf. EC 4.2.1.165
739109
Chlorobaculum tepidum WT2321
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
4.2.1.169
35
-
assay at; assay at
Chlorobaculum tepidum
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.2.1.169
7.8
-
assay at; assay at
Chlorobaculum tepidum
Cloned(Commentary) (protein specific)
EC Number
Commentary
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
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
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 (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.2.1.169
chlorosome
-
Chlorobaculum tepidum
46858
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.169
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
-
-
?
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-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
-
-
-
?
4.2.1.165
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
-
-
-
?
4.2.1.165
3-vinyl-8-propyl-12-ethyl-bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
(31R)-(1-hydroxyethyl)-8-propyl-12-ethyl-bacteriochlorophyllide d
-
-
-
?
4.2.1.165
chlorophyllide a + H2O
-
739109
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
-
739109
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
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
4.2.1.169
a 3-vinyl bacteriochlorophyllide a + H2O
-
739109
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
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
4.2.1.169
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
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
739109
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
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
4.2.1.169
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
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
739109
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
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
4.2.1.169
chlorophyllide a + H2O
cf. EC 4.2.1.165
739109
Chlorobaculum tepidum
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
4.2.1.169
chlorophyllide a + H2O
cf. EC 4.2.1.165
739109
Chlorobaculum tepidum WT2321
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
4.2.1.169
35
-
assay at
Chlorobaculum tepidum
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.2.1.169
7.8
-
assay at
Chlorobaculum tepidum
Expression
EC Number
Organism
Commentary
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
Commentary
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; 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; 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; 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 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; 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
General Information (protein specific)
EC Number
General Information
Commentary
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 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
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
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
Expression (protein specific)
EC Number
Organism
Commentary
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