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Information on EC 4.2.1.165 - chlorophyllide a 31-hydratase
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4.2.1.165 chlorophyllide a 31-hydrataseIUBMB Comments
The enzyme, together with EC 1.3.7.15, chlorophyllide-a reductase, and EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. The enzyme catalyses the hydration of a vinyl group on ring A, converting it to a hydroxyethyl group.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
3-vinyl hydratase, 3-vinyl-bacteriochlorophyll hydratase, bchf hydratase, 3-vinyl bacteriochlorophyllide a hydratase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-vinyl bacteriochlorophyllide hydratase
3-vinyl bacteriochlorophyllide a hydratase
3-vinyl hydratase
bacterial 3-vinyl hydratase
bchF
CT1421
3-vinyl bacteriochlorophyllide a hydratase
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
bchF
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a = 3-deacetyl-3-vinylbacteriochlorophyllide a + H2O
(2)
-
-
-
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a = chlorophyllide a + H2O
(1)
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
chlorophyllide-a 31-hydro-lyase
The enzyme, together with EC 1.3.7.15, chlorophyllide-a reductase, and EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. The enzyme catalyses the hydration of a vinyl group on ring A, converting it to a hydroxyethyl group.
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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 a + H2O
3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
r
3-vinyl bacteriochlorophyllide d + H2O
(3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
3-vinyl bacteriochlorophyllide d + H2O
(3RS)-3-(1-hydroxyethyl) bacteriochlorophyllide d
low activity, the enzyme converts [E,M], [E,E], [E,P], and [E,I] variants, 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
(31R)-(1-hydroxyethyl)-8-propyl-12-ethyl-bacteriochlorophyllide d
-
-
-
-
?
3-vinyl-8-propyl-12-ethyl-bacteriochlorophyllide d + H2O
(3RS)3-(1-hydroxyethyl)-8-propyl-12-ethyl-bacteriochlorophyllide d
-
-
-
?
3-vinyl-bacteriochlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
8-methylated 3-vinyl bacteriochlorophyllide d + H2O
?
the enzyme forms Zn-R[P,E]bacteriopheophorbide d as a major product and Zn-S[P,E]bacteriopheophorbide d as a minor one
-
-
?
bacteriochlorophyllide g + H2O
3-(1-hydroxyethyl) bacteriochlorophyllide g
-
-
-
r
chlorophyllide a + H2O
(31R)-3-(1-hydroxyethyl)-chlorophyllide a
-
-
formation of R-enantiomer at the 1-hydroxyethyl group is predominantly synthesized
-
?
12-methylated 3-vinyl bacteriochlorophyllide d + H2O
?
the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d
-
-
?
12-methylated 3-vinyl bacteriochlorophyllide d + H2O
?
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d
-
-
?
2-vinyl-bacteriochlorophyllide a + H2O
2-alpha-hydroxyethyl bacteriochlorophyllide a
-
-
-
?
2-vinyl-bacteriochlorophyllide a + H2O
2-alpha-hydroxyethyl bacteriochlorophyllide a
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
-
?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
high activity, preferred substrate
-
-
?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
high activity, preferred substrate
-
-
?
3-vinyl bacteriochlorophyllide c + H2O
(31RS)3-(1-hydroxyethyl) bacteriochlorophyllide c
-
-
-
?
3-vinyl bacteriochlorophyllide c + H2O
(31RS)3-(1-hydroxyethyl) bacteriochlorophyllide c
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
?
3-vinyl bacteriochlorophyllide d + H2O
(3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview
?
-
?
3-vinyl bacteriochlorophyllide d + H2O
(3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview
?
-
?
3-vinyl bacteriochlorophyllide d + H2O
(3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview
-
-
?
3-vinyl bacteriochlorophyllide d + H2O
(3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview
-
-
?
3-vinyl bacteriochlorophyllide d + H2O
(3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
-
reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview
?
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
3-vinyl-bacteriochlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
?
3-vinyl-bacteriochlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
a 3-vinyl bacteriochlorophyllide a + H2O
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
a 3-vinyl bacteriochlorophyllide a + H2O
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
when 3V-bacteriochlorophyllide a is used as a substrate, all enzyme homoluges are effective in in vitro hydration
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
-
when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration
-
-
?
chlorophyllide a + H2O
2-alpha-hydroxyethyl chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
2-alpha-hydroxyethyl chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
-
?
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
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
-
?
additional information
?
-
in bacteriochlorophyll a biosynthesis, 3-vinyl bacteriochlorophyllide a hydratase BchF converts the 3-hydroxyethyl group on pyrrole ring A into a 3-acetyl group
-
-
?
additional information
?
-
-
in bacteriochlorophyll a biosynthesis, 3-vinyl bacteriochlorophyllide a hydratase BchF converts the 3-hydroxyethyl group on pyrrole ring A into a 3-acetyl group
-
-
?
additional information
?
-
BchF catalyzes the hydration of hypomethylated bacteriochlorophyllide species to produce R-stereochemistry at C-31
-
-
?
additional information
?
-
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. BchF and BchV can recognize the Pi-conjugated system as their substrate and 17,18-dihydrogenation of porphyrin to chlorin Pi-system is necessary for the substrate of BchF- and BchV-hydration, BchF is active with chlorin and bacteriochlorin in the Pi-conjugate, while BchV is only active with chlorin in the Pi-conjugate, both do not use the porphyrin Pi-conjugate, overview
-
-
?
additional information
?
-
-
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. BchF and BchV can recognize the Pi-conjugated system as their substrate and 17,18-dihydrogenation of porphyrin to chlorin Pi-system is necessary for the substrate of BchF- and BchV-hydration, BchF is active with chlorin and bacteriochlorin in the Pi-conjugate, while BchV is only active with chlorin in the Pi-conjugate, both do not use the porphyrin Pi-conjugate, overview
-
-
?
additional information
?
-
coupled enzymatic assays of BchF and BchC are initiated in an anoxic chamber, using either crude cellular BchF and BchC extracts or alternatively a BchF extract and the purified BchC protein, with dithionite as an artificial electron donor (NAD+/NADP+ in in vivo assays), dithiothreitol, ATP, and an ATP-regenerating system (creatine phosphate and creatine phosphokinase) for the analysis of BchC (EC 1.1.1.396) substrate specificity, overview
-
-
?
additional information
?
-
-
coupled enzymatic assays of BchF and BchC are initiated in an anoxic chamber, using either crude cellular BchF and BchC extracts or alternatively a BchF extract and the purified BchC protein, with dithionite as an artificial electron donor (NAD+/NADP+ in in vivo assays), dithiothreitol, ATP, and an ATP-regenerating system (creatine phosphate and creatine phosphokinase) for the analysis of BchC (EC 1.1.1.396) substrate specificity, overview
-
-
?
additional information
?
-
in vitro activity measurements with crude enzyme extract
-
-
?
additional information
?
-
the secondary alcoholic hydroxy group is requisite for chlorosomal aggregation and biosynthesized by hydrating the 3-vinyl group of their precursors through chlorophyllide a 31-hydratase and 3-vinyl bacteriochlorophyllide d 31-hydratase. The enzyme catalyzes stereoselective hydration of zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c to the zinc (31R)-bacteriopheophorbide c homologue, with a slight amount of the (31S)-epimeric species. R-stereoselectivity is observed in the BchF-hydration of zinc 3-vinyl-8-ethyl-12-ethyl-bacteriopheophorbides c. The wild-type strain gives almost exclusively (31R)-epimers of 8-ethyl-12-methyl-(R[E,M]BChl c) and 8,12-diethyl-BChl c (R[E,E]BChl c), approximately 90% (31R)- and 10% (31S)-epimers of 8-propyl-12-ethyl-BChl c (R[P,E]BChl c and S[P,E]BChl c), and entirely 31S-epimer of 8-isobutyl-12-ethyl-BChl c (S[I,E]BChl c), 4% 31S-epimers in the total amount of BChl c homologues
-
-
?
additional information
?
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
coupled enzymatic assays of BchF and BchC are initiated in an anoxic chamber, using either crude cellular BchF and BchC extracts or alternatively a BchF extract and the purified BchC protein, with dithionite as an artificial electron donor (NAD+/NADP+ in in vivo assays), dithiothreitol, ATP, and an ATP-regenerating system (creatine phosphate and creatine phosphokinase) for the analysis of BchC (EC 1.1.1.396) substrate specificity, overview
-
-
?
additional information
?
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
in vitro activity measurements with crude enzyme extract
-
-
?
additional information
?
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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. BchF and BchV can recognize the Pi-conjugated system as their substrate and 17,18-dihydrogenation of porphyrin to chlorin Pi-system is necessary for the substrate of BchF- and BchV-hydration, BchF is active with chlorin and bacteriochlorin in the Pi-conjugate, while BchV is only active with chlorin in the Pi-conjugate, both do not use the porphyrin Pi-conjugate, overview
-
-
?
additional information
?
-
in bacteriochlorophyll a biosynthesis, 3-vinyl bacteriochlorophyllide a hydratase BchF converts the 3-hydroxyethyl group on pyrrole ring A into a 3-acetyl group
-
-
?
additional information
?
-
BchF catalyzes the hydration of hypomethylated bacteriochlorophyllide species to produce R-stereochemistry at C-31
-
-
?
additional information
?
-
-
the enzyme BchF produces an approximately 9:1 mixture of 31R- and S-epimers of the product
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 a + H2O
3-(1-hydroxyethyl) bacteriochlorophyllide a
-
-
-
r
3-vinyl bacteriochlorophyllide d + H2O
(3RS)-3-(1-hydroxyethyl) bacteriochlorophyllide d
low activity, the enzyme converts [E,M], [E,E], [E,P], and [E,I] variants, 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-vinyl-bacteriochlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
bacteriochlorophyllide g + H2O
3-(1-hydroxyethyl) bacteriochlorophyllide g
-
-
-
r
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
-
-
-
?
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
-
-
-
-
?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
?
3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
-
?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
high activity, preferred substrate
-
-
?
3-vinyl bacteriochlorophyllide a + H2O
(31RS)-3-(1-hydroxyethyl) bacteriochlorophyllide a
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
high activity, preferred substrate
-
-
?
3-vinyl bacteriochlorophyllide c + H2O
(31RS)3-(1-hydroxyethyl) bacteriochlorophyllide c
-
-
-
?
3-vinyl bacteriochlorophyllide c + H2O
(31RS)3-(1-hydroxyethyl) bacteriochlorophyllide c
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
?
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
-
-
-
?
3-vinyl-bacteriochlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
?
3-vinyl-bacteriochlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
a 3-vinyl bacteriochlorophyllide a + H2O
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
a 3-vinyl bacteriochlorophyllide a + H2O
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
when 3V-bacteriochlorophyllide a is used as a substrate, all enzyme homoluges are effective in in vitro hydration
-
-
?
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
a 3-vinyl bacteriochlorophyllide d + H2O
-
when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
-
?
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
-
-
-
?
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
-
-
-
?
additional information
?
-
in bacteriochlorophyll a biosynthesis, 3-vinyl bacteriochlorophyllide a hydratase BchF converts the 3-hydroxyethyl group on pyrrole ring A into a 3-acetyl group
-
-
?
additional information
?
-
-
in bacteriochlorophyll a biosynthesis, 3-vinyl bacteriochlorophyllide a hydratase BchF converts the 3-hydroxyethyl group on pyrrole ring A into a 3-acetyl group
-
-
?
additional information
?
-
BchF catalyzes the hydration of hypomethylated bacteriochlorophyllide species to produce R-stereochemistry at C-31
-
-
?
additional information
?
-
in bacteriochlorophyll a biosynthesis, 3-vinyl bacteriochlorophyllide a hydratase BchF converts the 3-hydroxyethyl group on pyrrole ring A into a 3-acetyl group
-
-
?
additional information
?
-
BchF catalyzes the hydration of hypomethylated bacteriochlorophyllide species to produce R-stereochemistry at C-31
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
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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
-
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
the organism contains three active enzyme homologues, ClimR0003, ClimR0008, and ClimR0017
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
BchF is predicted to have four transmembrane helices, suggesting that the later steps of bacteriochlorophyll a synthesis occur within the membrane
brenda
integral membrane protein, four putative membrane-spanning helices comprising the transmembrane segments Ile23-Tyr42,Thr56-Glu77, Phe94-Gln113, and His118-Gln140
brenda
integral transmembrane protein, the enzyme contains four putative membrane-spanning helices comprising the transmembrane segments Ile23-Tyr42, Thr56-Glu77, Phe94-Gln113, and His118-Gln140
brenda
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
integral transmembrane protein, the enzyme contains four putative membrane-spanning helices comprising the transmembrane segments Ile23-Tyr42, Thr56-Glu77, Phe94-Gln113, and His118-Gln140
-
brenda
-
integral membrane protein, four putative membrane-spanning helices comprising the transmembrane segments Ile23-Tyr42,Thr56-Glu77, Phe94-Gln113, and His118-Gln140
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
genotyping of single copy gene encoding BchF in Proteobacteria, Acidobacteria, Chloroflexi, and Gemmatimonadetes. Phototrophic Chlorobi usually carry two or three paralogues of BchF, with a second form named BchV. The different versions of BchF in Chlorobi are thought to aid in the synthesis of enantiomeric forms of bacteriochlorophyll c, d, and e that are characteristic of this phylum. Bacteriochlorophyll a cannot be synthetized without BchF and because BchF is only and exclusively found in those bacteria that make bacteriochlorophyll a, the phylogeny of this enzyme is, in consequence, the most direct piece of evidence for the origin of phototrophy based on bacteriochlorophyll a. Phylogenetic analysis, overview. The ancestral form of BchF originated early during the evolution of bacteria at a point in time that predated the diversification of the major groups of anoxygenic phototrophs
malfunction
metabolism
physiological function
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 [E,M]- and [E,E]BChl c, 9-12% S-stereochemistry in [P,E]BChl c, and nearly 100% S-stereochemistry in [I,E]BChl c
malfunction
deletion of gene bchF in a bacteriochlorophyll (BChl) b-producing strain of Rhodobacter sphaeroides leads to the production of an analogue of bacteriochlorophyllide g, BChl gP, where P is phytyl, rather than the native BChl aP. In the bchF-deletion mutant, hydration of the C3-vinyl group in 3-vinyl bacteriochlorophyllide a is blocked, but this precursor can be esterified with phytol. Enzyme BchF deletion- in the DELTAbciA/bchXYZBv background results in formation of BChl g esterified with phytol (BChl gP). Pigment analysis in several bch mutants, overview
malfunction
further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases. In vivo experiments with bchF-deleted mutants show considerably lower levels of bacteriochlorophyll a than the wild-type strain
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 showed a significant decrease of the S-epimers and accumulations of C3-vinyl BChl c species. In BChl a biosynthesis, the C3-vinyl group of a precursor of BChl a is hydrated by BchF, and the C3-1-hydroxyethyl group is then oxidized to the acetyl moiety by BchC
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 showed a significant decrease of the S-epimers and accumulations of C3-vinyl BChl c species. In BChl a biosynthesis, the C3-vinyl group of a precursor of BChl a is hydrated by BchF, and the C3-1-hydroxyethyl group is then oxidized to the acetyl moiety by BchC
-
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. In vivo experiments with bchF-deleted mutants show considerably lower levels of bacteriochlorophyll a than the wild-type strain
-
metabolism
BchF may specifically be required for bacteriochlorophyll a biosynthesis
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
the enzyme is involved in the biosynthetic pathways of different baceriochlorophyllides, e.g. a and g, overview
metabolism
-
BchF may specifically be required for bacteriochlorophyll a biosynthesis
-
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
-
a bacteriochlorophyll-less mutant of Rhodopseudomonas sphaeroides excretes tetrapyrrole-protein complex into the incubation medium. The major pigment of the complex is 2-desacetyl-2-vinylbacteriopheophorbide, indicating the existence of an alternate pathway of bacteriochlorophyll synthesis. This implies that reduction from the chlorin to the tetrahydroporphyrin stage can occur either before or after hydration of the 2-vinyl substituent of chlorophyllide a to an a-hydroxyethyl group. The mutant is presumably deficient in the enzyme responsible for hydration of the 2-vinyl to the 2-alpha-hydroxyethyl group
physiological function
bchF encodes a bacteriochlorophyll a-specific enzyme that adds water across the 2-vinyl group in bacteriochlorophyll synthesis
physiological function
-
deficiency in BchF impairs the production of both bacteriochlorophyllide a and bacteriochlorophyllide c.Pigment analyses of the BchF inactivated mutant, which still has BchV as a sole hydratase, shows higher ratios of S-epimeric bacteriochlorophyll c than the wild-type strain. The heightened prevalence of S-stereoisomers in the mutant is more remarkable at lower light intensities and causes a red shift of the chlorosomal Qy absorption band leading to advantages for light-energy transfer
physiological function
in the bacteriochlorophyll a biosynthetic pathway, hydration of the C-3 vinyl group is catalyzed by BchF. Chlorobium tepidum gene bchF complements Rhodobacter capsulatus strains defective in specific steps of bacteriochlorophyll a biosynthesis
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 bacteriochlorophyll a and other chlorosomal pigments considering the substrate specificity and stereoselectivity, and comparisons of by 3-vinyl hydratases derived from green sulfur bacteria, overview. Chloroflexus aurantiacus possesses a 2:1 mixture of R/S[E,M]BChls c
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
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
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])bacteriochlorophyll c, is a 9:1 mixture of 31R- and 31S-epimers, and bacteriochlorophyll c species with one more 82-methylation, 8-isobutyl-12-ethyl-([I,E])bacteriochlorophyll c, predominantly produces a 31S-epimer. Both BchF and BchV can hydrate the 3-vinyl group of chlorophyllide a as a substrate of the hydratases in the bacteriochlorophyll a biosynthetic pathway. Both BchF and BchV play a role in bacteriochlorophyll a biosynthesis, but BchF has a lower substrate specificity to the precursors of bacteriochlorophyll a than BchV
physiological function
bacteriochlorophyll a requires formation of a 3-hydroxyethyl group on pyrrole ring A that is subsequently converted into a 3-acetyl group by 3-vinyl bacteriochlorophyllide a hydratase (BchF) followed by 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC)
physiological function
gene bchF encodes an enzyme responsible for the hydration of the C3-vinyl group of a precursor of bacteriochlorophylls
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
physiological function
the photosynthetic green sulfur bacterium Chlorobaculum 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
-
in the bacteriochlorophyll a biosynthetic pathway, hydration of the C-3 vinyl group is catalyzed by BchF. Chlorobium tepidum gene bchF complements Rhodobacter capsulatus strains defective in specific steps of bacteriochlorophyll a biosynthesis
-
physiological function
-
bchF encodes a bacteriochlorophyll a-specific enzyme that adds water across the 2-vinyl group in bacteriochlorophyll synthesis
-
physiological function
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
bacteriochlorophyll a requires formation of a 3-hydroxyethyl group on pyrrole ring A that is subsequently converted into a 3-acetyl group by 3-vinyl bacteriochlorophyllide a hydratase (BchF) followed by 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC)
-
physiological function
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
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
-
physiological function
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
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])bacteriochlorophyll c, is a 9:1 mixture of 31R- and 31S-epimers, and bacteriochlorophyll c species with one more 82-methylation, 8-isobutyl-12-ethyl-([I,E])bacteriochlorophyll c, predominantly produces a 31S-epimer. Both BchF and BchV can hydrate the 3-vinyl group of chlorophyllide a as a substrate of the hydratases in the bacteriochlorophyll a biosynthetic pathway. Both BchF and BchV play a role in bacteriochlorophyll a biosynthesis, but BchF has a lower substrate specificity to the precursors of bacteriochlorophyll a than BchV
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G2LJR9_CHLTF
Chloracidobacterium thermophilum (strain B)
181
0
21423
TrEMBL
-
H2VFK0_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
158
0
18396
TrEMBL
-
BCHF_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
171
0
19254
Swiss-Prot
-
BCHF_CERS4
Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)
160
0
17984
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q8KBL0_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
190
0
22260
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 20008, sequence calculation, x * 25000, recombinant His6-tagged enzyme, SDS-PAGE
?
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
x * 20008, sequence calculation, x * 25000, recombinant His6-tagged enzyme, SDS-PAGE
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
deletion of gene bchF in a BChl b-producing strain of Rhodobacter sphaeroides leads to the production of an analogue of bacteriochlorophyllide g, BChl gP, where P is phytyl, rather than the native BChl aP. In the bchF-deletion mutant, hydration of the C3-vinyl group in 3-vinyl bacteriochlorophyllide a is blocked, but this precursor can be esterified with phytol. Enzyme BchF deletion- in the DELTAbciA/bchXYZBv background results in formation of BChl g esterified with phytol (BChl gP)
additional information
bchF deletion mutant, mutant phenotype with altered pigment biosynthesis, detailed overview
additional information
reconstitution of a bacteriochlorophyll formation pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC, with chlorin 3-hydroxyethyl chlorophyllide as a natural substrate identified for BchC. Modification of the isocyclic E ring, omission of the central magnesium ion, zinc as an alternative metal ion, and a non-reduced B ring system are tolerated by BchC. According to this broadened in vitro activity, the chlorin 3-hydroxyethyl chlorophyllide a is identified as a natural substrate of BchC in a reconstituted pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC. The established reaction sequence allows for an additional new branching point for the synthesis of bacteriochlorophyll a
additional information
-
reconstitution of a bacteriochlorophyll formation pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC, with chlorin 3-hydroxyethyl chlorophyllide as a natural substrate identified for BchC. Modification of the isocyclic E ring, omission of the central magnesium ion, zinc as an alternative metal ion, and a non-reduced B ring system are tolerated by BchC. According to this broadened in vitro activity, the chlorin 3-hydroxyethyl chlorophyllide a is identified as a natural substrate of BchC in a reconstituted pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC. The established reaction sequence allows for an additional new branching point for the synthesis of bacteriochlorophyll a
additional information
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
reconstitution of a bacteriochlorophyll formation pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC, with chlorin 3-hydroxyethyl chlorophyllide as a natural substrate identified for BchC. Modification of the isocyclic E ring, omission of the central magnesium ion, zinc as an alternative metal ion, and a non-reduced B ring system are tolerated by BchC. According to this broadened in vitro activity, the chlorin 3-hydroxyethyl chlorophyllide a is identified as a natural substrate of BchC in a reconstituted pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC. The established reaction sequence allows for an additional new branching point for the synthesis of bacteriochlorophyll a
-
additional information
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
bchF deletion mutant, mutant phenotype with altered pigment biosynthesis, detailed overview
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) is efficiently isolated by detergent solubilization and ultracentrifugation from the host membrane fraction
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bchF, phylogenetic analysis, recombinant expression in Escherichia coli strain Bl21(DE3), quantitative RT-PCR expression analysis
gene bchF, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene bchF, the enzyme is encoded in an operon, bchF-bchC-bchX,with two other single-copy genes required for BChl a biosynthesis
single copy gene, genotyping of BchF in Proteobacteria, Acidobacteria, Chloroflexi, and Gemmatimonadetes, phylogenetic analysis
gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3)
-
gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Burke, D.H.; Alberti, M.; Hearst, J.E.
bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants
J. Bacteriol.
175
2414-2422
1993
Rhodobacter capsulatus (P26165), Rhodobacter capsulatus ATCC BAA-309 (P26165)
brenda
Pudek, M.; Richards, W.
A possible alternate pathway of bacteriochlorophyll biosynthesis in a mutant of Rhodopseudomonas sphaeroides
Biochemistry
14
3132-3137
1975
Cereibacter sphaeroides
brenda
Lange, C.; Kiesel, S.; Peters, S.; Virus, S.; Scheer, H.; Jahn, D.; Moser, J.
Broadened substrate specificity of 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC) indicates a new route for the biosynthesis of bacteriochlorophyll a
J. Biol. Chem.
290
19697-19709
2015
Chlorobaculum tepidum (H2VFK0), Chlorobaculum tepidum, Chlorobaculum tepidum DSM 12025 (H2VFK0)
brenda
Harada, J.; Teramura, M.; Mizoguchi, T.; Tsukatani, Y.; Yamamoto, K.; Tamiaki, H.
Stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyll c by the hydratases BchF and BchV: adaptation of green sulfur bacteria to limited-light environments
Mol. Microbiol.
98
1184-1198
2015
Chlorobaculum tepidum
brenda
Frigaard, N.; Gomez Maqueo Chew, A.; Li, H.; Maresca, J.; Bryant, D.
Chlorobium tepidum: insights into the structure, physiology, and metabolism of a green sulfur bacterium derived from the complete genome sequence
Photosynth. Res.
78
93-117
2003
Chlorobaculum tepidum (H2VFK0), Chlorobaculum tepidum DSM 12025 (H2VFK0)
brenda
Ortega-Ramos, M.; Canniffe, D.; Radle, M.; Neil Hunter, C.; Bryant, D.; Golbeck, J.
Engineered biosynthesis of bacteriochlorophyll gF in Rhodobacter sphaeroides
Biochim. Biophys. Acta
1859
501-509
2018
Cereibacter sphaeroides (Q53222)
-
brenda
Lange, C.; Kiesel, S.; Peters, S.; Virus, S.; Scheer, H.; Jahn, D.; Moser, J.
Broadened substrate specificity of 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC) indicates a new route for the biosynthesis of bacteriochlorophyll a
J. Biol. Chem.
290
19697-19709
2015
Chlorobaculum tepidum (Q8KBL0), Chlorobaculum tepidum, Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS (Q8KBL0)
brenda
Harada, J.; Teramura, M.; Mizoguchi, T.; Tsukatani, Y.; Yamamoto, K.; Tamiaki, H.
Stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyll c by the hydratases BchF and BchV adaptation of green sulfur bacteria to limited-light environments
Mol. Microbiol.
98
1184-1198
2015
Chlorobaculum tepidum (Q8KBL0), Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS (Q8KBL0)
brenda
Teramura, M.; Harada, J.; Tamiaki, H.
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
Photosynth. Res.
130
33-45
2016
Chlorobaculum tepidum (Q8KBL0)
brenda
Teramura, M.; Harada, J.; Tamiaki, H.
In vitro enzymatic assays of photosynthetic bacterial 3-vinyl hydratases for bacteriochlorophyll biosyntheses
Photosynth. Res.
135
319-328
2018
Chloroflexus aurantiacus, Chlorobaculum limnaeum (A0A1D8D5T2), Chlorobaculum limnaeum, Chloracidobacterium thermophilum (G2LJR9), Chloracidobacterium thermophilum, Chlorobaculum tepidum (Q8KBL0), Chlorobaculum tepidum, Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS (Q8KBL0)
brenda
Cardona, T.
Origin of bacteriochlorophyll a and the early diversification of photosynthesis
PLoS ONE
11
e0151250
2016
Chloracidobacterium thermophilum (G2LJR9)
brenda
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