BRENDA - Enzyme Database
show all sequences of 4.2.1.169

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:

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
-
-
?
additional information
Chlorobaculum tepidum
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlorobaculum tepidum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a 3-vinyl bacteriochlorophyllide d + H2O
-
748858
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
additional information
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
748858
Chlorobaculum tepidum
?
-
-
-
-
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
?
-
-
-
-
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d + H2O
-
748858
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide d
-
-
-
?
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
-
-
?
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a 3-vinyl bacteriochlorophyllide d + H2O
-
748858
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
additional information
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
748858
Chlorobaculum tepidum
?
-
-
-
-
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
?
-
-
-
-
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d + H2O
-
748858
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide d
-
-
-
?
Expression
Organism
Commentary
Expression
Chlorobaculum tepidum
the transcriptional level of bchV gene is upregulated under low light conditions
up
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Expression (protein specific)
Organism
Commentary
Expression
Chlorobaculum tepidum
the transcriptional level of bchV gene is upregulated under low light conditions
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
-
-
-
-
-
-
-
-
12
-
1
-
-
-
1
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
6
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
13
-
-
-
-
-
-
-
-
-
1
3
3
1
-
-
741110
Frigaard
Chlorobium tepidum: insights i ...
Chlorobaculum tepidum, Chlorobaculum tepidum DSM 12025
Photosyn. Res.
78
93-117
2003
-
-
1
-
1
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
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-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-