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Information on EC 4.2.1.169 - 3-vinyl bacteriochlorophyllide d 31-hydratase
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4.2.1.169 3-vinyl bacteriochlorophyllide d 31-hydrataseIUBMB Comments
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is involved in the biosynthesis of bacteriochlorophylls c, d and e. It acts in the direction of hydration, and the hydroxyl group that is formed is essential for the ability of the resulting bacteriochlorophylls to self-aggregate in the chlorosomes, unique light-harvesting antenna structures found in these organisms. The product is formed preferentially in the (R)-configuration.
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The expected taxonomic range for this enzyme is: Chlorobaculum tepidum
Reaction Schemes
Synonyms
c3-vinyl hydratase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-vinyl hydratase
bacterial 3-vinyl hydratase
bacteriochlorophyll c3(1) hydratase
bchF
BchV
C3-vinyl hydratase
chV
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CT1776
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 3-(1-hydroxyethyl) bacteriochlorophyllide d = a 3-vinyl bacteriochlorophyllide d + H2O
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PATHWAY SOURCE
PATHWAYS
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, ,
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SYSTEMATIC NAME
IUBMB Comments
3-vinylbacteriochlorophyllide-d 31-hydro-lyase
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is involved in the biosynthesis of bacteriochlorophylls c, d and e. It acts in the direction of hydration, and the hydroxyl group that is formed is essential for the ability of the resulting bacteriochlorophylls to self-aggregate in the chlorosomes, unique light-harvesting antenna structures found in these organisms. The product is formed preferentially in the (R)-configuration.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
3-vinyl bacteriochlorophyllide d + H2O
(3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
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reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview
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-
?
3-vinyl bacteriochlorophyllide d + H2O
(3RS)-3-(1-hydroxyethyl) bacteriochlorophyllide d
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high activity, the enzyme converts [E,M], [E,E], [P,E], and [E,I] variants, the [E,E] and [P,E] variants are preferred substrates, stereochemistry, overview
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?
3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
3-vinyl-8-isobutyl-12-ethyl-bacteriochlorophyllide d + H2O
(31RS)3-(1-hydroxyethyl) bacteriochlorophyllide d
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-
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?
3-vinyl-8-propyl-12-ethyl-bacteriochlorophyllide d + H2O
(3RS)3-(1-hydroxyethyl)-8-propyl-12-ethyl-bacteriochlorophyllide d
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?
8-methylated 3-vinyl bacteriochlorophyllide d + H2O
?
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the enzyme forms Zn-R[P,E]bacteriopheophorbide d as a major product and Zn-S[P,E]bacteriopheophorbide d as a minor one
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?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide d + H2O
zinc (31R)-8-ethyl-12-methyl-bacteriopheophorbide d + zinc (31S)-8-ethyl-12-methyl-bacteriopheophorbide d
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-
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?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
12-methylated 3-vinyl bacteriochlorophyllide d + H2O
?
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the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d
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-
?
12-methylated 3-vinyl bacteriochlorophyllide d + H2O
?
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d
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-
?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
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?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
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?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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-
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?
3-vinyl bacteriochlorophyllide c + H2O
(31S)-3-(1-hydroxyethyl) bacteriochlorophyllide c
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low activity
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?
3-vinyl bacteriochlorophyllide c + H2O
(31S)-3-(1-hydroxyethyl) bacteriochlorophyllide c
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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low activity
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?
3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
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-
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?
3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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?
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
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?
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
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?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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?
a 3-vinyl bacteriochlorophyllide a + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
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?
a 3-vinyl bacteriochlorophyllide a + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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?
a 3-vinyl bacteriochlorophyllide a + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
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?
a 3-vinyl bacteriochlorophyllide a + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
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?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
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?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
cf. EC 4.2.1.165
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?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
cf. EC 4.2.1.165
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?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
BchV-hydration gives a relatively larger amount of the 31S epimers
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?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
R-stereoselectivity of BchF
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?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
Chlorobaculum tepidum ATCC 49652
R-stereoselectivity of BchF
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-
?
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
Chlorobaculum tepidum ATCC 49652
BchV-hydration gives a relatively larger amount of the 31S epimers
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?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
BchV-hydration gives a relatively larger amount of the 31S epimers
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?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
R-stereoselectivity of BchF
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-
?
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
Chlorobaculum tepidum ATCC 49652
BchV-hydration gives a relatively larger amount of the 31S epimers
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?
additional information
?
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the enzyme is a bacteriochlorophyllide c-specific BchF paralogue, cf. EC 4.2.1.165. BchV catalyzes the hydration of the C-3 vinyl group of highly methylated bacteriochlorophyllide species to produce S-stereochemistry
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?
additional information
?
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the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
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?
additional information
?
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the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
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?
additional information
?
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the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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both BchF and BchV from Chlorobaculum tepidum catalyze in vitro hydration of the 3-vinyl group of Zn-3V-[E,M]bacteriopheophorbide d. The reaction of Zn-3V-[E,E]bacteriopheophorbide d, the 121-methylated derivative of Zn-3V-[E,M]bacteriopheophorbides d, shows two products assigned to a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d. The R-epimeric product is predominant. Zn-3V-[P,E]bacteriopheophorbide d, the homologue methylated at the 82-position of Zn-3V-[E,E]bacteriopheophorbide d as a substrate gives similar results to that of Zn-3V-[E,E]bacteriopheophorbide d. Both BchF and BchV hydrate Zn-3V-[P,E]bacteriopheophorbide d stereoselectively and produce Zn-R[P,E]bacteriopheophorbide d as a major product and Zn-S[P,E]bacteriopheophorbide d as a minor one. With one more 82-methylated pigment, Zn-3V-[I,E]bacteriopheophorbide d, both BchF and BchV hydrate the 3-vinyl group of the substrate. No activity of BchF or BchV with Zn-3V-[I,E]bacteriopheophorbide c, the 20-methylated derivative of Zn-3V-[I,E]bacteriopheophorbide d
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?
additional information
?
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in vitro activity measurements with crude enzyme extract
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additional information
?
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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
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?
additional information
?
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Chlorobaculum tepidum ATCC 49652
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
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?
additional information
?
-
Chlorobaculum tepidum ATCC 49652
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
-
-
?
additional information
?
-
Chlorobaculum tepidum ATCC 49652
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
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?
additional information
?
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Chlorobaculum tepidum ATCC 49652
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
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?
additional information
?
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Chlorobaculum tepidum ATCC 49652
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
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-
?
additional information
?
-
Chlorobaculum tepidum ATCC 49652
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
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-
?
additional information
?
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Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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in vitro activity measurements with crude enzyme extract
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-
?
additional information
?
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Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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both BchF and BchV from Chlorobaculum tepidum catalyze in vitro hydration of the 3-vinyl group of Zn-3V-[E,M]bacteriopheophorbide d. The reaction of Zn-3V-[E,E]bacteriopheophorbide d, the 121-methylated derivative of Zn-3V-[E,M]bacteriopheophorbides d, shows two products assigned to a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d. The R-epimeric product is predominant. Zn-3V-[P,E]bacteriopheophorbide d, the homologue methylated at the 82-position of Zn-3V-[E,E]bacteriopheophorbide d as a substrate gives similar results to that of Zn-3V-[E,E]bacteriopheophorbide d. Both BchF and BchV hydrate Zn-3V-[P,E]bacteriopheophorbide d stereoselectively and produce Zn-R[P,E]bacteriopheophorbide d as a major product and Zn-S[P,E]bacteriopheophorbide d as a minor one. With one more 82-methylated pigment, Zn-3V-[I,E]bacteriopheophorbide d, both BchF and BchV hydrate the 3-vinyl group of the substrate. No activity of BchF or BchV with Zn-3V-[I,E]bacteriopheophorbide c, the 20-methylated derivative of Zn-3V-[I,E]bacteriopheophorbide d
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?
additional information
?
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the enzyme is a bacteriochlorophyllide c-specific BchF paralogue, cf. EC 4.2.1.165. BchV catalyzes the hydration of the C-3 vinyl group of highly methylated bacteriochlorophyllide species to produce S-stereochemistry
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
3-vinyl bacteriochlorophyllide d + H2O
(3RS)-3-(1-hydroxyethyl) bacteriochlorophyllide d
-
high activity, the enzyme converts [E,M], [E,E], [P,E], and [E,I] variants, the [E,E] and [P,E] variants are preferred substrates, stereochemistry, overview
-
-
?
3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
3-vinyl-8-isobutyl-12-ethyl-bacteriochlorophyllide d + H2O
(31RS)3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
-
?
3-vinyl-8-propyl-12-ethyl-bacteriochlorophyllide d + H2O
(3RS)3-(1-hydroxyethyl)-8-propyl-12-ethyl-bacteriochlorophyllide d
-
-
-
-
?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
-
?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
-
?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
-
?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
-
?
3-vinyl bacteriochlorophyllide c + H2O
(31S)-3-(1-hydroxyethyl) bacteriochlorophyllide c
-
low activity
-
-
?
3-vinyl bacteriochlorophyllide c + H2O
(31S)-3-(1-hydroxyethyl) bacteriochlorophyllide c
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
low activity
-
-
?
3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
-
-
-
-
?
3-vinyl-8,12-diethyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8,12-diethyl-bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
-
?
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
-
-
-
-
?
3-vinyl-8-ethyl-12-methyl-bacteriochlorophyllide d + H2O
(31R)-(1-hydroxyethyl)-8-ethyl-12-methyl-bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
-
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
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-
?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
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-
?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652
enzyme BchV prefers the S-stereoisomer, stereospecific reaction
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
bacteriochlorophyllide d is converted to bacteriochlorophyllide c
-
-
?
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
cf. EC 4.2.1.165
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
cf. EC 4.2.1.165
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-
?
additional information
?
-
the enzyme is a bacteriochlorophyllide c-specific BchF paralogue, cf. EC 4.2.1.165. BchV catalyzes the hydration of the C-3 vinyl group of highly methylated bacteriochlorophyllide species to produce S-stereochemistry
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-
?
additional information
?
-
-
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
-
-
?
additional information
?
-
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Chlorobaculum tepidum ATCC 49652
the in vitro stereoselective hydration confirms the in vivo production of the S-epimeric species by BchV
-
-
?
additional information
?
-
the enzyme is a bacteriochlorophyllide c-specific BchF paralogue, cf. EC 4.2.1.165. BchV catalyzes the hydration of the C-3 vinyl group of highly methylated bacteriochlorophyllide species to produce S-stereochemistry
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the central metal of substrates is essential for the BchF reaction
additional information
the central metal of substrates is essential for the BchF reaction
additional information
the central metal of substrates is essential for the BchV reaction
additional information
the central metal of substrates is essential for the BchV reaction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
phylogenetic relationships of BchF and BchV orthologues, overview
evolution
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phylogenetic relationships of BchF and BchV orthologues, overview
-
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
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
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
malfunction
in the bchV knockout mutant strain, about 85% of the total BChl c is normal, except that the most highly methylated species (8-iso-butyl, 12-ethyl BChl c), normally observed in the wild-type strain, is absent. The mutant shows the changes in BChl c aggregation and absorption properties, light harvesting and growth at low light intensities are seriously impaired in the bchV mutant
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
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
malfunction
-
further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases
malfunction
-
pigment analyses of the bchF-inactivated mutant, which still has BchV as a sole hydratase, show higher ratios of S-epimeric bacteriochlorophyll c than the wild-type strain, while the bchV-mutant possessing only BchF shows a significant decrease of the S-epimers and accumulations of C3-vinyl BChl c species
malfunction
Chlorobaculum tepidum ATCC 49652
-
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
-
malfunction
Chlorobaculum tepidum ATCC 49652
-
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
-
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
-
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
-
malfunction
-
in the bchV knockout mutant strain, about 85% of the total BChl c is normal, except that the most highly methylated species (8-iso-butyl, 12-ethyl BChl c), normally observed in the wild-type strain, is absent. The mutant shows the changes in BChl c aggregation and absorption properties, light harvesting and growth at low light intensities are seriously impaired in the bchV mutant
-
malfunction
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
pigment analyses of the bchF-inactivated mutant, which still has BchV as a sole hydratase, show higher ratios of S-epimeric bacteriochlorophyll c than the wild-type strain, while the bchV-mutant possessing only BchF shows a significant decrease of the S-epimers and accumulations of C3-vinyl BChl c species
-
malfunction
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases
-
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
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
metabolism
-
enzyme involvement in the biosynthetic pathways of BChl c homologues and epimers, overview
metabolism
-
proposed biosynthetic pathways of bacteriochlorophyllides a and c focused on Chlorobaculum tepidum BchF- and BchV-catalyzed reactions, overview
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
-
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
-
metabolism
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
proposed biosynthetic pathways of bacteriochlorophyllides a and c focused on Chlorobaculum tepidum BchF- and BchV-catalyzed reactions, overview
-
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
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
physiological function
-
a chlorosome is a large and efficient light-harvesting antenna system found in some photosynthetic bacteria. This system comprises self-aggregates of bacteriochlorophyll (BChl) c, d, or e possessing a chiral 1-hydroxyethyl group at the 3-position, which plays a key role in the formation of the supramolecule. Biosynthesis of chlorosomal pigments involves stereoselective conversion of 3-vinyl group to 3-(1-hydroxyethyl) group facilitated by a 3-vinyl hydratase. This 3-vinyl hydration also occurs in BChl a biosynthesis, followed by oxidation that introduces an acetyl group at the 3-position catalyzed by 3-vinyl hydratases. Analysis of the biosynthetic pathway of BChl a and other chlorosomal pigments considering the substrate specificity and stereoselectivity, and comparisons of by 3-vinyl hydratases derived from green sulfur bacteria, overview. The green sulfur bacterium Chlorobaculum tepidum synthesizes three types of chlorophyllous pigments: Chl aPD (Chl a esterified with DELTA2,6-phytadienol), BChl a, and BChl c. The core part of chlorosomes in Chlorobaculum tepidum consists of self-aggregates of BChl c molecules, which are a mixture of 31R/S-epimers as well as a mixture of 82-and 121-methylated homologues. In the cells, the chiral 31-carbon of BChl c species possessing the 8-ethyl group, 8-ethyl-12-methyl-([E,M]), and 8,12-diethyl-([E,E])BChls c, exclusively shows R-stereochemistry. The single 82-methylated species, 8-propyl-12-ethyl-([P,E])BChl c, is a 9:1 mixture of 31R- and 31S-epimers, and BChl c species with one more 82-methylation, 8-isobutyl-12-ethyl-([I,E])BChl c, predominantly produces a 31S-epimer. Both BchF and BchV can hydrate the 3-vinyl group of Chlide a as a substrate of the hydratases in the BChl a biosynthetic pathway
physiological function
-
photosynthetic green sulfur bacteria inhabit anaerobic environments with very low-light conditions. Stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyll c by the hydratases BchF and BchV (EC 4.2.1.169) for adaptation of green sulfur bacteria to limited-light environments. The pigment possess a hydroxy group at the C31 position that produces a chiral center with R- or S-stereochemistry and the C31-hydroxy group serves as a connecting moiety for the self-aggregation. Transcriptional level of bchV is upregulated at lower light intensity, the Chlorobaculum tepidum adapts to low-light environments by control of the bchV transcription
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
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
-
physiological function
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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
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physiological function
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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photosynthetic green sulfur bacteria inhabit anaerobic environments with very low-light conditions. Stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyll c by the hydratases BchF and BchV (EC 4.2.1.169) for adaptation of green sulfur bacteria to limited-light environments. The pigment possess a hydroxy group at the C31 position that produces a chiral center with R- or S-stereochemistry and the C31-hydroxy group serves as a connecting moiety for the self-aggregation. Transcriptional level of bchV is upregulated at lower light intensity, the Chlorobaculum tepidum adapts to low-light environments by control of the bchV transcription
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physiological function
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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a chlorosome is a large and efficient light-harvesting antenna system found in some photosynthetic bacteria. This system comprises self-aggregates of bacteriochlorophyll (BChl) c, d, or e possessing a chiral 1-hydroxyethyl group at the 3-position, which plays a key role in the formation of the supramolecule. Biosynthesis of chlorosomal pigments involves stereoselective conversion of 3-vinyl group to 3-(1-hydroxyethyl) group facilitated by a 3-vinyl hydratase. This 3-vinyl hydration also occurs in BChl a biosynthesis, followed by oxidation that introduces an acetyl group at the 3-position catalyzed by 3-vinyl hydratases. Analysis of the biosynthetic pathway of BChl a and other chlorosomal pigments considering the substrate specificity and stereoselectivity, and comparisons of by 3-vinyl hydratases derived from green sulfur bacteria, overview. The green sulfur bacterium Chlorobaculum tepidum synthesizes three types of chlorophyllous pigments: Chl aPD (Chl a esterified with DELTA2,6-phytadienol), BChl a, and BChl c. The core part of chlorosomes in Chlorobaculum tepidum consists of self-aggregates of BChl c molecules, which are a mixture of 31R/S-epimers as well as a mixture of 82-and 121-methylated homologues. In the cells, the chiral 31-carbon of BChl c species possessing the 8-ethyl group, 8-ethyl-12-methyl-([E,M]), and 8,12-diethyl-([E,E])BChls c, exclusively shows R-stereochemistry. The single 82-methylated species, 8-propyl-12-ethyl-([P,E])BChl c, is a 9:1 mixture of 31R- and 31S-epimers, and BChl c species with one more 82-methylation, 8-isobutyl-12-ethyl-([I,E])BChl c, predominantly produces a 31S-epimer. Both BchF and BchV can hydrate the 3-vinyl group of Chlide a as a substrate of the hydratases in the BChl a biosynthetic pathway
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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
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
additional information
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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
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
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
additional information
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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
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
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
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
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
additional information
Chlorobaculum tepidum ATCC 49652
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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
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additional information
Chlorobaculum tepidum ATCC 49652
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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
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additional information
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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]BCh