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Literature summary for 2.5.1.115 extracted from

  • Collakova, E.; DellaPenna, D.
    Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis (2001), Plant Physiol., 127, 1113-1124.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.115

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Arabidopsis thaliana
expression in Escherichia coli Synechocystis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Arabidopsis thaliana 16020
-
membrane membrane-bound Synechocystis sp. 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phytyl diphosphate + homogentisate Arabidopsis thaliana the enzyme is involved in the biosynthesis of the vitamin E tocopherols diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
-
 ?
phytyl diphosphate + homogentisate Synechocystis sp. the enzyme is involved in the biosynthesis of the vitamin E tocopherols diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8VWJ1
-
-
Synechocystis sp. P73726
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranylgeranyl diphosphate + homogentisate about 18% of the activity with phythyldiphosphate Synechocystis sp. diphosphate + 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2
-
 ?
geranylgeranyl diphosphate + homogentisate
-
 Synechocystis sp. ?
-
 ?
additional information no substrate: solanesyl diphosphate Synechocystis sp. ?
-
 ?
phytyl diphosphate + homogentisate preferred substrate Synechocystis sp. diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
-
 ?
phytyl diphosphate + homogentisate the enzyme is involved in the biosynthesis of the vitamin E tocopherols Arabidopsis thaliana diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
-
 ?
phytyl diphosphate + homogentisate the enzyme is involved in the biosynthesis of the vitamin E tocopherols Synechocystis sp. diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
-
 ?
phytyl diphosphate + homogentisate no activity with geranylgeranyl diphosphate, no activity with solanesyl diphosphate Arabidopsis thaliana diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
-
 ?
phytyl diphosphate + homogentisate phytyl diphosphate and homogentisate are the preferred substrates in vito, no activity with solanesyl diphosphate Synechocystis sp. diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
-
 ?

Synonyms

Synonyms Comment Organism
HPT
-
 Arabidopsis thaliana
SynHPT
-
 Synechocystis sp.
VTE2
-
 Arabidopsis thaliana
VTE2
-
 Synechocystis sp.

General Information

General Information Comment Organism
malfunction disruption of Synechocystis sp. PCC 6803 HPT function causes an absence of tocopherols without affecting plastoquinone-9 levels, indicating that separate polyprenyltransferases exist for tocopherol and plastoquinone synthesis in Synechocystis sp. PCC 6803 Synechocystis sp.
physiological function the enzyme is involved in the biosynthesis of the vitamin E tocopherols. Tocopherol functions to limit lipid oxidation during seed desiccation, quiescence and germination and early seedling development. Protects thylakoid membrane lipids from photooxidation and is required for low-temperature adaptation Arabidopsis thaliana
physiological function the enzyme is involved in the biosynthesis of the vitamin E tocopherols. Tocopherol functions to limit lipid oxidation during seed desiccation, quiescence and germination and early seedling development. Protects thylakoid membrane lipids from photooxidation and is required for low-temperature adaptation Synechocystis sp.
physiological function SLR1736 gene disruption does not lead to significant differences in cellular plastoquinone, phylloquinone, and chlorophyll levels, but causes absence of tocopherols without affecting plastoquinone-9 levels Synechocystis sp.