Abstract
Prenyltransferases (PTs) are enzymes that catalyze prenyl chain elongation. Some are highly similar to each other at the amino acid level. Therefore, it is difficult to assign their function based solely on their sequence homology to functional orthologs. Other experiments, such as in vitro enzymatic assay, mutant analysis, and mutant complementation are necessary to assign their precise function. Moreover, subcellular localization can also influence the functionality of the enzymes within the pathway network, because different isoprenoid end products are synthesized in the cytosol, mitochondria, or plastids from prenyl diphosphate (prenyl-PP) substrates. In addition to in vivo functional experiments, in silico approaches, such as co-expression analysis, can provide information about the topology of PTs within the isoprenoid pathway network. There has been huge progress in the last few years in the characterization of individual Arabidopsis PTs, resulting in better understanding of their function and their topology within the isoprenoid pathway. Here, we summarize these findings and present the updated topological model of PTs in the Arabidopsis thaliana isoprenoid pathway.
Highlights
Isoprenoids form a large group of more than 55,000 natural metabolites despite the fact that they are all derived from just five carbon units of isopentenyl diphosphate (IPP) [1]
IPP is a prenyl acceptor of the prenyl group originating from DMAPP, in the reaction catalyzed by PTs
Members of the short-chain ones are in ascending order C10 geranyl geranyl diphosphate synthase (GPPS), C15 farnesyl diphosphate synthase (FPPS), C20 geranylgeranyl diphosphate synthase (GPPS), C15 farnesyl diphosphate synthase (FPPS), C20 geranylgeranyl diphosphate synthase (GGPPS), and C25 geranylfarnesyl diphosphate synthase (GFPPS) (Table 1)
Summary
Isoprenoids form a large group of more than 55,000 natural metabolites despite the fact that they are all derived from just five carbon units of isopentenyl diphosphate (IPP) [1]. IPP and its isomer dimethylallyl diphosphate (DMAPP) are synthetized in a highly conserved manner in almost all living species. In plants, they are produced in the cytosol via the mevalonic acid (MVA) pathway and in plastids through the MVA-independent methylerythritol phosphate (MEP) pathway. PTs are any enzymes that catalyze the transfer of the prenyl group [3]. 22 of of 25 review, we will use the term PT for convenience, as PT is more frequently used in the literature, but refer to only the prenyl chain elongating enzymes that catalyze sequential condensation of allylic we will refer to only the prenyl chain elongating enzymes that catalyze sequential condensation of diphosphate and IPP
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