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:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chlorosome
;
Chlorobaculum tepidum
46858
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
the central metal of substrates is essential for the BchF reaction; the central metal of substrates is essential for the BchV reaction
Chlorobaculum tepidum
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
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum ATCC 49652
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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
?
-
-
-
additional information
Chlorobaculum tepidum ATCC 49652
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
H2VFK0
-
-
Chlorobaculum tepidum
Q8KBL0
-
-
Chlorobaculum tepidum ATCC 49652
H2VFK0
-
-
Chlorobaculum tepidum ATCC 49652
Q8KBL0
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a 3-vinyl bacteriochlorophyllide d + H2O
-
741107
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
741107
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
-
741107
Chlorobaculum tepidum ATCC 49652
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
741107
Chlorobaculum tepidum ATCC 49652
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
741107
Chlorobaculum tepidum
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchF catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchF in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchF hydration. In all the BchF-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers. The 20-methylated analogue of Zn-3V[E,M]BPheide d, Zn-3V[E,M]BPheide c, is hydrated by BchF and BchV enzymes to give Zn-[E,M]BPheide c
741107
Chlorobaculum tepidum
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchV catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively, with a slight amount of the 31S-epimeric species. The BchV-hydration gives a relatively larger amount of the 31S-epimers. The in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchV in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchV hydration. In all the BchV-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers
741107
Chlorobaculum tepidum
?
-
-
-
-
additional information
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
741107
Chlorobaculum tepidum ATCC 49652
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchF catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchF in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchF hydration. In all the BchF-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers. The 20-methylated analogue of Zn-3V[E,M]BPheide d, Zn-3V[E,M]BPheide c, is hydrated by BchF and BchV enzymes to give Zn-[E,M]BPheide c
741107
Chlorobaculum tepidum ATCC 49652
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchV catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively, with a slight amount of the 31S-epimeric species. The BchV-hydration gives a relatively larger amount of the 31S-epimers. The in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchV in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchV hydration. In all the BchV-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers
741107
Chlorobaculum tepidum ATCC 49652
?
-
-
-
-
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
R-stereoselectivity of BchF
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
R-stereoselectivity of BchF
741107
Chlorobaculum tepidum ATCC 49652
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum ATCC 49652
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
R-stereoselectivity of BchF
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum ATCC 49652
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
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
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chlorosome
-
Chlorobaculum tepidum
46858
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
the central metal of substrates is essential for the BchF reaction
Chlorobaculum tepidum
additional information
the central metal of substrates is essential for the BchV reaction
Chlorobaculum tepidum
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
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum ATCC 49652
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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
?
-
-
-
additional information
Chlorobaculum tepidum ATCC 49652
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
-
741107
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
741107
Chlorobaculum tepidum
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
-
741107
Chlorobaculum tepidum ATCC 49652
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
741107
Chlorobaculum tepidum ATCC 49652
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
741107
Chlorobaculum tepidum
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchF catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchF in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchF hydration. In all the BchF-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers. The 20-methylated analogue of Zn-3V[E,M]BPheide d, Zn-3V[E,M]BPheide c, is hydrated by BchF and BchV enzymes to give Zn-[E,M]BPheide c
741107
Chlorobaculum tepidum
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchV catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively, with a slight amount of the 31S-epimeric species. The BchV-hydration gives a relatively larger amount of the 31S-epimers. The in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchV in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchV hydration. In all the BchV-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers
741107
Chlorobaculum tepidum
?
-
-
-
-
additional information
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
741107
Chlorobaculum tepidum ATCC 49652
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchF catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchF in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchF hydration. In all the BchF-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers. The 20-methylated analogue of Zn-3V[E,M]BPheide d, Zn-3V[E,M]BPheide c, is hydrated by BchF and BchV enzymes to give Zn-[E,M]BPheide c
741107
Chlorobaculum tepidum ATCC 49652
?
-
-
-
-
additional information
in vitro enzymatic hydration of some 3-vinyl-chlorophyll derivatives with usage of zinc complexes of cyclic tetrapyrroles as the enzymatic substrates alternative to chlorophyll(ide)s chelated with magnesium ion. Recombinant BchV catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c or d to the zinc 31R-bacteriopheophorbide c or d homologue, respectively, with a slight amount of the 31S-epimeric species. The BchV-hydration gives a relatively larger amount of the 31S-epimers. The in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV. The enzymatic hydration for the 8-propylated substrate proceeds more slowly than that for the 8-ethylated, and the 8-isobutylated substrate is no longer hydrated. The wild-type strain of Chlorobaculum tepidum gives almost exclusively 31R-epimers of 8-ethyl-12-methyl- and 8,12-diethyl-BChl c, approximately 90% 31R- and 10% 31S-epimers of 8-propyl-12-ethyl-BChl c, and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c: 4% 31S-epimers in the total amount of BChl c homologues. The in vivo hydrations might be effective even after the 20-methylation by a methyltransferase, BchU. No activity of BchV in the hydration of the 3-vinyl group of protochlorophyllide a, the porphyrin form of chlorophyllide a. The hydrogenation of the porphyrin to chlorin Pi-system is necessary for the substrate of BchV hydration. In all the BchV-catalyzed reactions, the products are mixtures of the 31R- and 31S-epimers, and the R-epimers are mainly obtained with a lower amount of the S-epimers
741107
Chlorobaculum tepidum ATCC 49652
?
-
-
-
-
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
R-stereoselectivity of BchF
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
R-stereoselectivity of BchF
741107
Chlorobaculum tepidum ATCC 49652
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum ATCC 49652
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
R-stereoselectivity of BchF
741107
Chlorobaculum tepidum
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
BchV-hydration gives a relatively larger amount of the 31S epimers
741107
Chlorobaculum tepidum ATCC 49652
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
-
-
-
?
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
the transcriptional level of bchV gene is upregulated under low light conditions
up
General Information
General Information
Commentary
Organism
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 8-ethyl-12-methyl- and 8,12-diethyl-BChls c, 9-12% S-stereochemistry in 8-propyl-12-ethyl-BChl c, and nearly 100% S-stereochemistry in 8-isobutyl-12-ethyl-BChl c; 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 8-ethyl-12-methyl- and 8,12-diethyl-BChls c, 0-6% S-stereochemistry in 8-propyl-12-ethyl-BChl c, and very few 8-isobutyl-12-ethyl-BChl c
Chlorobaculum tepidum
additional information
the central metal is essential for the BchF reaction. Since the 132-methoxycarbonyl group in substrates is not necessary for the enzymatic reactions, the free 172-carboxy group and the central magnesium ion of chlorins are important for the substrates of hydration by BchF enzyme; the central metal is essential for the BchV reaction. Since the 132-methoxycarbonyl group in substrates is not necessary for the enzymatic reactions, the free 172-carboxy group and the central magnesium ion of chlorins are important for the substrates of hydration by BchV enzyme
Chlorobaculum tepidum
General Information (protein specific)
General Information
Commentary
Organism
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 8-ethyl-12-methyl- and 8,12-diethyl-BChls c, 9-12% S-stereochemistry in 8-propyl-12-ethyl-BChl c, and nearly 100% S-stereochemistry in 8-isobutyl-12-ethyl-BChl c
Chlorobaculum tepidum
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 8-ethyl-12-methyl- and 8,12-diethyl-BChls c, 0-6% S-stereochemistry in 8-propyl-12-ethyl-BChl c, and very few 8-isobutyl-12-ethyl-BChl c
Chlorobaculum tepidum
additional information
the central metal is essential for the BchF reaction. Since the 132-methoxycarbonyl group in substrates is not necessary for the enzymatic reactions, the free 172-carboxy group and the central magnesium ion of chlorins are important for the substrates of hydration by BchF enzyme
Chlorobaculum tepidum
additional information
the central metal is essential for the BchV reaction. Since the 132-methoxycarbonyl group in substrates is not necessary for the enzymatic reactions, the free 172-carboxy group and the central magnesium ion of chlorins are important for the substrates of hydration by BchV enzyme
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
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1
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6
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12
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2
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741107
Teramura
In vitro stereospecific hydrat ...
Chlorobaculum tepidum, Chlorobaculum tepidum ATCC 49652
Photosyn. Res.
130
33-45
2016
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1
1
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8
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4
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21
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21
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2
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2
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1
2
4
1
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748858
Teramura
In vitro stereospecific hydra ...
Chlorobaculum tepidum
Photosyn. Res.
130
33-45
2016
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1
3
3
1
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739109
Harada
Stereochemical conversion of C ...
Chlorobaculum tepidum, Chlorobaculum tepidum WT2321
Mol. Microbiol.
98
1184-1198
2015
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1
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1
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1
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6
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8
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14
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2
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1
5
10
1
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748684
Harada
Stereochemical conversion of ...
Chlorobaculum tepidum, Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
Mol. Microbiol.
98
1184-1198
2015
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1
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1
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11
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7
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11
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13
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1
3
3
1
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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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