2.1.1.295: 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase
This is an abbreviated version!
For detailed information about 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.295
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2.1.1.295
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tocopherol
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gamma-tocopherols
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plastoquinone
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methyltransferases
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agriculture
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synechocystis
- 2.1.1.295
- tocopherol
- gamma-tocopherols
- plastoquinone
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methyltransferases
- agriculture
- synechocystis
Reaction
Synonyms
2-methyl-6-phytyl-1, 4-benzoquinol methyltransferase, 2-methyl-6-phytyl-1,4- benzoquinol methyltransferase, 2-methyl-6-phytyl-1,4-benzoquinol methyltransferase, 2-methyl-6-phytylbenzoquinone methyltransferase, 2-methyl-6-solanyl-1,4-hydroquinone methyltransferase, LSMT, MPBQ methyltransferase, MPBQ MT, MPBQ-MT, MPBQ/MSBQ methyltransferase, MPBQ/MSBQ MT, MPBQ/MSBQ transferase, MT-1, MT-2, SLL0418 protein, VTE3
ECTree
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General Information
General Information on EC 2.1.1.295 - 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase
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evolution
malfunction
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an SLL0418 partial knockout mutant accumulates beta-tocopherol with no effect in the overall tocopherol content of the cell
metabolism
physiological function
Arachis hypogaea ssp. fastigiata
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the cultivated peanut Arachis hypogaea might originate via hybridization of Arachis duranensis (A-genome) and Arachis ipaensis (B-genome), followed by a rare spontaneous duplication of chromosomes, phylogenetic analysis
evolution
the cultivated peanut Arachis hypogaea might originate via hybridization of Arachis duranensis (A-genome) and Arachis ipaensis (B-genome), followed by a rare spontaneous duplication of chromosomes, phylogenetic analysis
evolution
the cultivated peanut Arachis hypogaea might originate via hybridization of Arachis duranensis (A-genome) and Arachis ipaensis (B-genome), followed by a rare spontaneous duplication of chromosomes, phylogenetic analysis
evolution
the cultivated peanut Arachis hypogaea might originate via hybridization of Arachis duranensis (A-genome) and Arachis ipaensis (B-genome), followed by a rare spontaneous duplication of chromosomes, phylogenetic analysis
evolution
the enzyme has the typical functional domains of an SAM enzyme
Arachis hypogaea ssp. fastigiata
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2-methyl-6-phytyl-1,4-benzoquinol methyltransferase is one of the critical enzymes involved in vitamin E biosynthesis in plants. The enzyme can catalyze 2-methyl-6-phytyl-1,4-benzoquinol to generate 2,3-dimethyl-6-phytyl-1,4-benzoquinone. Both compounds are cyclized by tocopherol cyclase to yield delta- and gamma-tocopherol, respectively, which are subsequently further converted to beta- and alpha-tocopherol by gamma-tocopherol methyltransferase
metabolism
2-methyl-6-phytyl-1,4-benzoquinol methyltransferase is one of the critical enzymes involved in vitamin E biosynthesis in plants. The enzyme can catalyze 2-methyl-6-phytyl-1,4-benzoquinol to generate 2,3-dimethyl-6-phytyl-1,4-benzoquinone. Both compounds are cyclized by tocopherol cyclase to yield delta- and gamma-tocopherol, respectively, which are subsequently further converted to beta- and alpha-tocopherol by gamma-tocopherol methyltransferase
metabolism
2-methyl-6-phytyl-1,4-benzoquinol methyltransferase is one of the critical enzymes involved in vitamin E biosynthesis in plants. The enzyme can catalyze 2-methyl-6-phytyl-1,4-benzoquinol to generate 2,3-dimethyl-6-phytyl-1,4-benzoquinone. Both compounds are cyclized by tocopherol cyclase to yield delta- and gamma-tocopherol, respectively, which are subsequently further converted to beta- and alpha-tocopherol by gamma-tocopherol methyltransferase
metabolism
2-methyl-6-phytyl-1,4-benzoquinol methyltransferase is one of the critical enzymes involved in vitamin E biosynthesis in plants. The enzyme can catalyze 2-methyl-6-phytyl-1,4-benzoquinol to generate 2,3-dimethyl-6-phytyl-1,4-benzoquinone. Both compounds are cyclized by tocopherol cyclase to yield delta- and gamma-tocopherol, respectively, which are subsequently further converted to beta- and alpha-tocopherol by gamma-tocopherol methyltransferase
metabolism
2-methyl-6-phytyl-1,4-benzoquinol methyltransferase (MPBQ-MT) is a vital enzyme catalyzing a key methylation step in both alpha/gamma-tocopherol and plastoquinone biosynthetic pathway
metabolism
the enzyme is involved in regulation and biosynthesis of vitamin E in safflower
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the enzyme is involved in the biosynthesis of plastoquinol, as well as vitamin E (tocopherols and tocotrienols)
physiological function
an isoform MT-1 homozygous mutant is non-lethal and produces 24-45% alpha-tocopherol and 55-74% beta-tocopherol as compared to 96% alpha- and 4% beta-tocopherol for wild-type
physiological function
isoform MT-2 compensates for the loss of isoform MT-1 function, and the MT-2 mutation profoundly affects the synthesis of tocopherols without adversely affecting the synthesis of plastoquinone crucial for normal plant growth and development
physiological function
loss of enzymic activity results in accumulation of delta-tocopherol and decreased gamma-tocopherol content in the seed
physiological function
loss-of-function mutant seedlings are pale green and do not survive beyond 7 days in soil. Mutation does not affect embryo growth and development
physiological function
2-methyl-6-phytyl-1,4-benzoquinol methyltransferase (MPBQ-MT) is a vital enzyme catalyzing a key methylation step in both alpha/gamma-tocopherol and plastoquinone biosynthetic pathway. Overexpression of LsMT significantly increases plastoquinone (PQ) level in lettuce. The increase of tocopherol and plastoquinone levels by LsMT overexpression conduce to the improvement of plants' tolerance and photosynthesis under high light stress, by directing excessive light energy toward photosynthetic production rather than toward generation of more photooxidative damage. No significant difference in the expression levels of HPPD, HPT, TC and gamma-TMT is observed between wild-type and transgenic plants, indicating that overexpression of LsMT does not impact on the expression of other genes up- and downstream in the tocopherol biosynthetic pathway. Mechanism by which overexpression of MPBQ-MT leads to enhanced photosynthesis and tolerance to photodamage under high light in lettuce, overview