isoprenoid biosynthetic process

Despite their diverse chemical structures, most of the known plant hormones are derived from three main types of metabolic precursors: amino acids, isoprenoid compounds, and lipids (Figure A3.1). The amino acids tryptophan and methionine serve as precursors for IAA (indole-3-acetic acid) and ethylene, respectively. The isoprenoid pathway gives rise to five classes of plant hormones: cytokinins, brassinosteroids, gibberellins, abscisic acid, and strigolactones. And finally, jasmonic acid is synthesized from a lipid precursor.

isoprenoid biosynthetic process via mevalonate (1)

T1 - Synthesis and activity of fluorescent isoprenoid pyrophosphate analogues

isoprenoid biosynthetic process via 1-deoxy-D-xylulose 5-phosphate

This review focuses on progress in our understanding of how the precursors for isoprenoid biosynthesis are synthesized in the two subcellular compartments, how the underlying pathway gene networks are organized and regulated, and how network perturbations impact each pathway and plant development.

Biosynthesis of Cholesterol, Steroids, and Isoprenoids

Because of the wealth of data on isoprenoid biosynthesis, we emphasize research in Arabidopsis thaliana and compare the synthesis of isoprenoid precursor molecules in this model plant with their synthesis in other prokaryotic and eukaryotic organisms.

Biosynthesis of polyisoprenoid alcohols and their biologicalrole have been reviewed in 2005 ().

Special Issues - Molecules - MDPI

Isoprenoid compounds (also referred to as terpenoids) are synthesized from isoprene subunits via the mevonolate and methylerythritol phosphate pathways in the chloroplasts and cytosol of plants. Isoprenoid precursors are used to synthesize four major plant hormones.

Molecules, an international, peer-reviewed Open Access journal.

The immediate products of the IPT reaction are iP-ribotides. The isoprene side chain of iP-ribotides is subsequently trans-hydroxylated by the P450 monooxygenases CYP735A1 and CYP735A2 to yield zeatin ribotides (Takei et al. 2004). Cytokinin nucleotides can be converted to their most active free base forms via dephosphorylation and deribosylation. Such interconversions may involve enzymes common to purine metabolism. In addition to these enzymes, the monophosphate forms of cytokinin ribotides can be directly converted to the free base forms by the phosphoribohydrolase LONELY GUY (LOG) (see Figure A3.5), which was identified in a rice mutant that displayed shoot meristem defects (Kurakawa et al. 2007). LOG expression is localized to the tip of shoot meristems and the enzyme likely fine-tunes the spatial distribution of bioactive cytokinins to regulate meristem activity. Zeatin can be oxidized; it can also be conjugated to form O-glucosides or N-glucosides. These reactions are shown in Figures A3.6 and A3.7.

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Synthesis and Evaluation of Alkyne Contaning Isoprenoid Analogue

Unlike isoprenoid biosynthesis in other living organisms, prenyl-PP, as the precursor of all isoprenoids in plants, is synthesized by two independent pathways: the mevalonate (MVA) pathway in the cytoplasm and the 2- C -methyl- d -erythritol 4-phosphate (MEP) pathway in plastids.

15/05/2013 · Metabolic plasticity for isoprenoid biosynthesis in bacteria

isoprenoid biosynthetic process

GAs, like all terpenoid compounds, are made from five-carbon isoprenoid building blocks. GAs are diterpenoids that are formed from four isoprenoid units. The GA biosynthetic pathway can be divided into three stages, each residing in a different cellular compartment: plastid, ER, or cytosol (Figure A3.9).

Synthesis and activity of fluorescent isoprenoid pyrophosphate analogues

fatty alcohols and aldehydes - Lipid

The chloroplast methylerythritol phosphate pathway is the primary source of the DMAPP used in cytokinin biosynthesis by plant IPT enzymes. This pathway occurs in plastids, which is where the majority of IPT enzymes are localized in plants. Thus, the primary site of cytokinin biosynthesis in plants is in the plastids. However, in Arabidopsis, at least one IPT protein, IPT3, can be modified by the addition of a farnesyl moiety (Galichet et al. 2008). Farnesylation is the addition of a hydrophobic farnesyl group (a long-chain lipid molecule made from isoprene subunits) to C-terminal cysteine(s) of the target protein, which can alter its subcellular localization, often targeting the protein to a membrane. The farnesylation of IPT3 directs it to the nucleus, rather than to the plastids, where the non-farnesylated IPT3 protein is localized. Furthermore, the IPT4 protein is found in the cytoplasm, and the IPT7 protein is found in mitochondria. Thus, the plastids are the primary sites of cytokinin biosynthesis, but not the only sites.