1.3.1.111: geranylgeranyl-bacteriochlorophyllide a reductase
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For detailed information about geranylgeranyl-bacteriochlorophyllide a reductase, go to the full flat file.
Reaction
Synonyms
BchP, geranylgeranyl-bacteriochlorophyll reductase, geranylgeranyl-bacteriopheophytin reductase, GG-Bphe reductase
ECTree
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General Information
General Information on EC 1.3.1.111 - geranylgeranyl-bacteriochlorophyllide a reductase
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malfunction
metabolism
physiological function
a mutant in orf391 synthesizes bacteriochlorophyll a that is esterified with geranylgeraniol rather than the normal phytol. Strains that accumulate geranylgeraniol-esterified bacteriochlorophyll a exhibit reduced photosynthetic growth capability compared to that observed with the parent strain which synthesizes bacteriochlorophyll a that is esterified with phytol. But synthesis of geranylgeranyl bacteriochlorophyllide a does not per se impair function of the reaction center complex nor energy transfer from the light harvesting complex
malfunction
a transposon mutant of gene bchP encoding geranylgeranyl-bacteriochlorophyll reductase possesses a structurally modified photosystem assembled with bacteriochlorophyll esterified with geranylgeraniol, rather than with phytol
malfunction
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex
malfunction
the CT2256-deleted mutant shows accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence, phenotype, overview
malfunction
the enzyme only catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin. It might be a naturally occurring bchP mutant with an insertion mutation that may have been the initial cause of a partial loss of function
malfunction
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the CT2256-deleted mutant shows accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence, phenotype, overview
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malfunction
Cereibacter sphaeroides NCIB 8253
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the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex
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malfunction
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a mutant in orf391 synthesizes bacteriochlorophyll a that is esterified with geranylgeraniol rather than the normal phytol. Strains that accumulate geranylgeraniol-esterified bacteriochlorophyll a exhibit reduced photosynthetic growth capability compared to that observed with the parent strain which synthesizes bacteriochlorophyll a that is esterified with phytol. But synthesis of geranylgeranyl bacteriochlorophyllide a does not per se impair function of the reaction center complex nor energy transfer from the light harvesting complex
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esterification of bacteriochlorophyllide a initially involves the addition of a geranylgeraniol group followed by sequential reduction of the geranylgeraniol moiety tophytol which is the end product of the pathway. Synthesis of geranylgeraniol-esterified bacteriochlorophyll does not affect the energy transfer rate from light harvesting to reaction center complexes nor the electron transfer function as measured by the yield of electron transfer to the primary and secondary quinones, the charge recombination rate from the quinones, and the rate of cytochrome c2 oxidation. Pathway for synthesis of bacteriochlorophyll from bacteriochlorophyllide, overview
metabolism
requirement of Rhodospirillum rubrum for phytylated bacteriopheophytin, a potential link between the absence of light-harvesting complex 2 and of phytylated bacteriochlorophyll from the wild-type bacterium. In addition to bacteriochlorophyll, the reaction center of purple bacteria contains two bacteriopheophytin molecules, one of which is the first clearly resolved acceptor of electrons, following electron transfer from the bacteriochlorophyll dimer. Proposed pathway for reduction of geranylgeranyl bacteriopheophytin a in Rhodospirillum rubrum, reduction proceeds via dihydro-GG-esterified and tetrahydro-GG-esterified intermediates to the final product, phytylated bacteriopheophytin
metabolism
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
metabolism
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis, pathway for the phytylation of bacteriochlorophyll a, overview
metabolism
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esterification of bacteriochlorophyllide a initially involves the addition of a geranylgeraniol group followed by sequential reduction of the geranylgeraniol moiety tophytol which is the end product of the pathway. Synthesis of geranylgeraniol-esterified bacteriochlorophyll does not affect the energy transfer rate from light harvesting to reaction center complexes nor the electron transfer function as measured by the yield of electron transfer to the primary and secondary quinones, the charge recombination rate from the quinones, and the rate of cytochrome c2 oxidation. Pathway for synthesis of bacteriochlorophyll from bacteriochlorophyllide, overview
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the bacteriochlorophyll of the purple photosynthetic bacterium Rhodobacter sphaeroides is esterified with phytol. The presence of this alcohol moiety is essential for the correct assembly of the photosynthetic apparatus. The enzyme is essential and responsible for the reduction of the alcohol moiety of (bacterio)chlorophyll to phytol
physiological function
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
physiological function
the enzyme is involved esterification of bacteriochlorophyll a with DELTA2,6-phytadienol and phytol, respectively, which is produced by reduction of the geranylgeranyl group at the C-17 propionate residue
physiological function
the enzyme is responsible for the reduction of the isoprenoid moiety of bacteriochlorophyll (Bchl) from geranylgeraniol (GG) to phytol, it also catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin
physiological function
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the enzyme is involved esterification of bacteriochlorophyll a with DELTA2,6-phytadienol and phytol, respectively, which is produced by reduction of the geranylgeranyl group at the C-17 propionate residue
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