This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: phytyl pyrophosphate biosynthesis, phytyl-PP biosynthesis
|Superclasses:||Biosynthesis → Secondary Metabolites Biosynthesis → Terpenoids Biosynthesis → Diterpenoids Biosynthesis → Phytyl Diphosphate Biosynthesis|
Some taxa known to possess this pathway include : Arabidopsis thaliana col
The phytyl chain is an essential component in the structure of diverse prenyllipids such as chlorophylls, tocopherols and phylloquinone [Keller98]. The phytyl chain allows for the insertion of those compounds into the hydrophobic core of membranes such as the plastid membrane of chloroplasts and etioplasts. To date, two pathways of prenylation have been described:
a) The first pathway concerns the prenylation of chlorophyllide a with geranylgeranyl diphosphate (GGPP) to form geranylgeranyl-chlorophyll a, which is subsequently converted through several successive steps of reduction to form chlorophyll a (see chlorophyll a biosynthesis II).
The former route was detected in plant etioplasts [Rudiger80], whilst the second was reported in chloroplasts, where the biosynthesis of tocopherol [Soll80] and phylloquinone [Schultz81] also utilizes preformed phytyl diphosphate.
In Arabidopsis thaliana a multifunctional enzyme was shown to be able to catalyze the multiple reduction steps in both routes: geranylgeranyl diphosphate to phytyl diphosphate as well as geranylgeranyl-chlorophyll a to chlorophyll a [Keller98].
Superpathways: superpathway of phylloquinol biosynthesis
Unification Links: AraCyc:PWY-5063
Keller98: Keller Y, Bouvier F, d'Harlingue A, Camara B (1998). "Metabolic compartmentation of plastid prenyllipid biosynthesis--evidence for the involvement of a multifunctional geranylgeranyl reductase." Eur J Biochem 251(1-2);413-7. PMID: 9492312
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