BRENDA - Enzyme Database
show all sequences of 4.2.1.169

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)
Commentary
Organism
gene bchF quantitative RT-PCR expression analysis, phylogenetic analysis; gene bchV, quantitative RT-PCR expression analysis, phylogenetic analysis
Chlorobaculum tepidum
Engineering
Amino acid exchange
Commentary
Organism
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
Localization
Commentary
Organism
GeneOntology No.
Textmining
chlorosome
;
Chlorobaculum tepidum
46858
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum
-
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum WT2321
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum WT2321
-
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
chlorophyllide a + H2O
Chlorobaculum tepidum
cf. EC 4.2.1.165
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
?
chlorophyllide a + H2O
Chlorobaculum tepidum WT2321
cf. EC 4.2.1.165
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlorobaculum tepidum
H2VFK0
gene bchF
-
Chlorobaculum tepidum
Q8KBL0
bchV
-
Chlorobaculum tepidum WT2321
H2VFK0
gene bchF
-
Chlorobaculum tepidum WT2321
Q8KBL0
bchV
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a 3-vinyl bacteriochlorophyllide a + H2O
-
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide a + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide a + H2O
-
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide a + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
chlorophyllide a + H2O
cf. EC 4.2.1.165
739109
Chlorobaculum tepidum
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
cf. EC 4.2.1.165
739109
Chlorobaculum tepidum WT2321
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
assay at; assay at
Chlorobaculum tepidum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at; assay at
Chlorobaculum tepidum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene bchF quantitative RT-PCR expression analysis, phylogenetic analysis
Chlorobaculum tepidum
gene bchV, quantitative RT-PCR expression analysis, phylogenetic analysis
Chlorobaculum tepidum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
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)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chlorosome
-
Chlorobaculum tepidum
46858
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum
-
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum WT2321
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum WT2321
-
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
chlorophyllide a + H2O
Chlorobaculum tepidum
cf. EC 4.2.1.165
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
?
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a 3-vinyl bacteriochlorophyllide a + H2O
-
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide a + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide a + H2O
-
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide a + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
-
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
739109
Chlorobaculum tepidum WT2321
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
chlorophyllide a + H2O
cf. EC 4.2.1.165
739109
Chlorobaculum tepidum
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
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)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
assay at
Chlorobaculum tepidum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Chlorobaculum tepidum
Expression
Organism
Commentary
Expression
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
General Information
Commentary
Organism
evolution
phylogenetic relationships of BchF and BchV orthologues, overview; phylogenetic relationships of BchF and BchV orthologues, overview
Chlorobaculum tepidum
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
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
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
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)
General Information
Commentary
Organism
evolution
phylogenetic relationships of BchF and BchV orthologues, overview
Chlorobaculum tepidum
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
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
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
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
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
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
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
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)
Organism
Commentary
Expression
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
Other publictions for EC 4.2.1.169
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748860
Teramura
In vitro enzymatic assays of ...
Chlorobaculum tepidum, Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
Photosyn. Res.
135
319-328
2018
-
-
1
-
-
-
1
-
-
1
-
6
-
3
-
-
-
-
-
-
-
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12
-
1
-
-
-
1
-
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-
-
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1
-
-
-
-
-
1
-
-
-
1
-
6
-
-
-
-
-
-
-
-
12
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
741107
Teramura
In vitro stereospecific hydrat ...
Chlorobaculum tepidum, Chlorobaculum tepidum ATCC 49652
Photosyn. Res.
130
33-45
2016
-
-
-
-
-
-
-
-
1
1
-
8
-
4
-
-
-
-
-
-
-
-
21
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
8
-
-
-
-
-
-
-
-
21
-
2
-
-
-
2
-
-
-
1
2
4
1
-
-
748858
Teramura
In vitro stereospecific hydra ...
Chlorobaculum tepidum
Photosyn. Res.
130
33-45
2016
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
3
3
1
-
-
739109
Harada
Stereochemical conversion of C ...
Chlorobaculum tepidum, Chlorobaculum tepidum WT2321
Mol. Microbiol.
98
1184-1198
2015
-
-
1
-
1
-
-
-
1
-
-
6
-
8
-
-
-
-
-
-
-
-
14
-
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
2
-
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6
-
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-
-
-
-
-
-
14
-
2
-
-
-
2
-
-
-
1
5
10
1
-
-
748684
Harada
Stereochemical conversion of ...
Chlorobaculum tepidum, Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
Mol. Microbiol.
98
1184-1198
2015
-
-
1
-
1
-
-
-
-
-
-
11
-
7
-
-
-
-
-
-
-
-
13
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
11
-
-
-
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741110
Frigaard
Chlorobium tepidum: insights i ...
Chlorobaculum tepidum, Chlorobaculum tepidum DSM 12025
Photosyn. Res.
78
93-117
2003
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