1.3.1.83: geranylgeranyl diphosphate reductase
This is an abbreviated version!
For detailed information about geranylgeranyl diphosphate reductase, go to the full flat file.
Word Map on EC 1.3.1.83
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1.3.1.83
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chlorophyll
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tocopherol
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phytyl
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phytolic
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geranylgeraniol
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light-harvesting
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protochlorophyllide
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bacteriochlorophyll
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tocotrienols
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acidocaldarius
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chlorophyllide
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light-harvesting-like
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phytoene
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phylloquinone
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chlorophyll-binding
- 1.3.1.83
- chlorophyll
- tocopherol
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phytyl
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phytolic
- geranylgeraniol
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light-harvesting
- protochlorophyllide
- bacteriochlorophyll
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tocotrienols
- acidocaldarius
- chlorophyllide
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light-harvesting-like
- phytoene
- phylloquinone
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chlorophyll-binding
Reaction
Synonyms
BchP, CHL P, ChlP, CT2256, geranylgeranyl reductase, GGPP reductase, GGR, GGR2, LYL1, NADPH-dependent geranylgeranyl reductase, PpCHL P
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General Information on EC 1.3.1.83 - geranylgeranyl diphosphate reductase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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highly conserved regions of characterized geranylgeranyl reductases, GGRs, from archaea, plants, and bacteria, overview
malfunction
metabolism
physiological function
additional information
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structural basis for recognition of a geranyl group by geranylgeranyl reductases, GGRs, overview
malfunction
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mass spectrometry reveals that cells deleted of HVO_1799 fail to fully reduce the isoprene chains of Hfx. volcanii membrane phospholipids and glycolipids. Likewise, the absence of HVO_1799 leads to a loss of saturation of the omega-position isoprene subunit of C55 and C60 dolichol phosphate, with the effect of HVO_1799 deletion being more pronounced with C60 dolichol phosphate than with C55 dolichol phosphate
malfunction
enzyme deficiency due to a recessive mutation G206S in gene CHLP leads to the yellow-green leaf mutant 502ys. The mutant exhibits reduced level of Chls, arrested development of chloroplasts, and retarded growth rate, phenotype, overview. The mutant phenotype is complemented by transformation with the wild-type gene
malfunction
the light-induced yellow leaf 1-1 (lyl1-1) mutant is hypersensitive to high-light and defective in the Chl synthesis. The mutation of LYL1 leads to conjugation of the majority of Chl molecules with an unsaturated geranylgeraniol side chain. The lyl1-1 mutant suffers from severe photooxidative damage and displays a drastic reduction in the levels of alpha-tocopherol and photosynthetic proteins. The yellowing of lyl1-1 mutant is caused by high-light stress. Mutant lyl1-1 phenotype, overview
malfunction
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mass spectrometry reveals that cells deleted of HVO_1799 fail to fully reduce the isoprene chains of Hfx. volcanii membrane phospholipids and glycolipids. Likewise, the absence of HVO_1799 leads to a loss of saturation of the omega-position isoprene subunit of C55 and C60 dolichol phosphate, with the effect of HVO_1799 deletion being more pronounced with C60 dolichol phosphate than with C55 dolichol phosphate
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metabolism
the enzyme is involved in the reduction step from Chl-geranylgeranylated (ChlGG) and geranylgeranyl diphosphate (GGPP) to Chl-phytol (ChlPhy) and phytyl diphosphate (PPP) in rice
metabolism
the three-step hydrogenation of geranylgeranyl diphosphate into phytyl diphosphate, and Chl-geranylgeranylated (ChlGG) and Chl-phytol (ChlPhy) is catalyzed by NADPH-dependent geranylgeranyl reductase. ENzyme LYL1 protects against lipid peroxidation and reactive oxygen species, ROS
physiological function
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DGGR catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
physiological function
geranylgeranyl reductase (CHL P) catalyzes the reduction of geranylgeranyl diphosphate to phytyl diphosphate, and provides phytol for both Chlorophyll (Chl) and tocopherol synthesis. The enzyme is involved in the reduction step from Chl-geranylgeranylated (ChlGG) and geranylgeranyl diphosphate (GGPP) to Chl-phytol (ChlPhy) and phytyl diphosphate (PPP) in rice
physiological function
the enzyme is involved in the reduction step from Chl-geranylgeranylated (ChlGG) and geranylgeranyl diphosphate (GGPP) to Chl-phytol (ChlPhy) and phytyl diphosphate (PPP) in rice. Enzyme LYL1 also plays an important role in response to high-light in rice
