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Literature summary extracted from

  • Teramura, M.; Harada, J.; Tamiaki, H.
    In vitro enzymatic assays of photosynthetic bacterial 3-vinyl hydratases for bacteriochlorophyll biosyntheses (2018), Photosynth. Res., 135, 319-328 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.165 gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) Chloroflexus aurantiacus
4.2.1.165 gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) Chlorobaculum tepidum
4.2.1.165 gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) Chloracidobacterium thermophilum
4.2.1.165 gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) Chlorobaculum limnaeum
4.2.1.169 gene bchF, recombinant overexpression in Escherichia coli strain BL21(DE3) Chlorobaculum tepidum

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.165 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 Chlorobaculum tepidum
4.2.1.169 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 Chlorobaculum tepidum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.165 Zn2+ required, substrate-bound Chloroflexus aurantiacus
4.2.1.165 Zn2+ required, substrate-bound Chlorobaculum tepidum
4.2.1.165 Zn2+ required, substrate-bound Chloracidobacterium thermophilum
4.2.1.165 Zn2+ required, substrate-bound Chlorobaculum limnaeum
4.2.1.169 Zn2+ required, substrate-bound Chlorobaculum tepidum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O Chloroflexus aurantiacus
-
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O Chlorobaculum tepidum
-
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O Chloracidobacterium thermophilum
-
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O Chlorobaculum limnaeum
-
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 a 3-(1-hydroxyethyl) bacteriochlorophyllide d Chlorobaculum limnaeum when 3V-bacteriochlorophyllide a is used as a substrate, all enzyme homoluges are effective in in vitro hydration a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.165 a 3-(1-hydroxyethyl) bacteriochlorophyllide d Chloroflexus aurantiacus when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.165 a 3-(1-hydroxyethyl) bacteriochlorophyllide d Chloracidobacterium thermophilum when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.165 chlorophyllide a + H2O Chloroflexus aurantiacus
-
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O Chlorobaculum tepidum
-
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O Chloracidobacterium thermophilum
-
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O Chlorobaculum limnaeum
-
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.169 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O Chlorobaculum tepidum
-
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.169 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.169 a 3-(1-hydroxyethyl) bacteriochlorophyllide d Chlorobaculum tepidum
-
a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.169 a 3-(1-hydroxyethyl) bacteriochlorophyllide d Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.169 chlorophyllide a + H2O Chlorobaculum tepidum
-
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.169 chlorophyllide a + H2O Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.165 Chloracidobacterium thermophilum G2LJR9
-
-
4.2.1.165 Chlorobaculum limnaeum A0A1D8D5T2 the organism contains three active enzyme homologues, ClimR0003, ClimR0008, and ClimR0017
-
4.2.1.165 Chlorobaculum tepidum Q8KBL0
-
-
4.2.1.165 Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS Q8KBL0
-
-
4.2.1.165 Chloroflexus aurantiacus
-
-
-
4.2.1.169 Chlorobaculum tepidum
-
-
-
4.2.1.169 Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.165 12-methylated 3-vinyl bacteriochlorophyllide d + H2O the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d Chlorobaculum tepidum ?
-
?
4.2.1.165 12-methylated 3-vinyl bacteriochlorophyllide d + H2O the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS ?
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
Chloroflexus aurantiacus 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
Chlorobaculum tepidum 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
Chloracidobacterium thermophilum 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
Chlorobaculum limnaeum 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.165 3-vinyl bacteriochlorophyllide d + H2O reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview Chlorobaculum tepidum (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
-
?
4.2.1.165 3-vinyl bacteriochlorophyllide d + H2O reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview Chloroflexus aurantiacus (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d ? ?
4.2.1.165 3-vinyl bacteriochlorophyllide d + H2O reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview Chloracidobacterium thermophilum (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d ? ?
4.2.1.165 3-vinyl bacteriochlorophyllide d + H2O reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview Chlorobaculum limnaeum (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d ? ?
4.2.1.165 3-vinyl bacteriochlorophyllide d + H2O reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
-
?
4.2.1.165 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 Chlorobaculum tepidum ?
-
?
4.2.1.165 a 3-(1-hydroxyethyl) bacteriochlorophyllide d when 3V-bacteriochlorophyllide a is used as a substrate, all enzyme homoluges are effective in in vitro hydration Chlorobaculum limnaeum a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.165 a 3-(1-hydroxyethyl) bacteriochlorophyllide d when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration Chloroflexus aurantiacus a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.165 a 3-(1-hydroxyethyl) bacteriochlorophyllide d when 3V-bacteriochlorophyllide a is used as a substrate, the enzyme is effective in in vitro hydration Chloracidobacterium thermophilum a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.165 chlorophyllide a + H2O
-
Chloroflexus aurantiacus 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O
-
Chlorobaculum tepidum 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O
-
Chloracidobacterium thermophilum 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O
-
Chlorobaculum limnaeum 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 chlorophyllide a + H2O
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.165 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 Chlorobaculum tepidum ?
-
?
4.2.1.165 additional information the enzyme BchF produces an approximately 9:1 mixture of 31R- and S-epimers of the product Chloroflexus aurantiacus ?
-
?
4.2.1.165 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 Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS ?
-
?
4.2.1.169 12-methylated 3-vinyl bacteriochlorophyllide d + H2O the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d Chlorobaculum tepidum ?
-
?
4.2.1.169 12-methylated 3-vinyl bacteriochlorophyllide d + H2O the enzyme forms a 31-epimeric mixture of Zn-R/S[E,E]bacteriopheophorbide d Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS ?
-
?
4.2.1.169 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
Chlorobaculum tepidum 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.169 3-deacetyl-3-vinyl-bacteriochlorophyllide a + H2O
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS 3-deacetyl-3-(1-hydroxyethyl)-bacteriochlorophyllide a
-
?
4.2.1.169 3-vinyl bacteriochlorophyllide d + H2O reaction mixture of Zn-3V-[E,M] or Zn-3V-[E,E]/[P,E]/[I,E]bacteriopheophorbide d homologues, overview Chlorobaculum tepidum (3R)-(1-hydroxyethyl) bacteriochlorophyllide d + (3S)-(1-hydroxyethyl) bacteriochlorophyllide d
-
?
4.2.1.169 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 Chlorobaculum tepidum ?
-
?
4.2.1.169 a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
Chlorobaculum tepidum a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.169 a 3-(1-hydroxyethyl) bacteriochlorophyllide d
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS a 3-vinyl bacteriochlorophyllide d + H2O
-
?
4.2.1.169 chlorophyllide a + H2O
-
Chlorobaculum tepidum 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.169 chlorophyllide a + H2O
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS 3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
-
?
4.2.1.169 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 Chlorobaculum tepidum ?
-
?
4.2.1.169 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 Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS ?
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.165 bacterial 3-vinyl hydratase
-
Chloroflexus aurantiacus
4.2.1.165 bacterial 3-vinyl hydratase
-
Chlorobaculum tepidum
4.2.1.165 bacterial 3-vinyl hydratase
-
Chloracidobacterium thermophilum
4.2.1.165 bacterial 3-vinyl hydratase
-
Chlorobaculum limnaeum
4.2.1.165 bchF
-
Chloroflexus aurantiacus
4.2.1.165 bchF
-
Chlorobaculum tepidum
4.2.1.165 bchF
-
Chloracidobacterium thermophilum
4.2.1.165 cfxBchF
-
Chloroflexus aurantiacus
4.2.1.165 ClimR0003
-
Chlorobaculum limnaeum
4.2.1.165 ClimR0008
-
Chlorobaculum limnaeum
4.2.1.165 ClimR0017
-
Chlorobaculum limnaeum
4.2.1.165 craBchF
-
Chloracidobacterium thermophilum
4.2.1.169 bacterial 3-vinyl hydratase
-
Chlorobaculum tepidum
4.2.1.169 BchV
-
Chlorobaculum tepidum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.165 35
-
assay at Chloroflexus aurantiacus
4.2.1.165 35
-
assay at Chlorobaculum tepidum
4.2.1.165 35
-
assay at Chloracidobacterium thermophilum
4.2.1.165 35
-
assay at Chlorobaculum limnaeum
4.2.1.169 35
-
assay at Chlorobaculum tepidum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.165 7.8
-
assay at Chloroflexus aurantiacus
4.2.1.165 7.8
-
assay at Chlorobaculum tepidum
4.2.1.165 7.8
-
assay at Chloracidobacterium thermophilum
4.2.1.165 7.8
-
assay at Chlorobaculum limnaeum
4.2.1.169 7.8
-
assay at Chlorobaculum tepidum

General Information

EC Number General Information Comment Organism
4.2.1.165 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 Chlorobaculum tepidum
4.2.1.165 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 Chloroflexus aurantiacus
4.2.1.165 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 Chloracidobacterium thermophilum
4.2.1.165 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 Chlorobaculum limnaeum
4.2.1.165 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 Chlorobaculum tepidum
4.2.1.169 malfunction further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases Chlorobaculum tepidum
4.2.1.169 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 Chlorobaculum tepidum