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Literature summary for 2.5.1.1 extracted from

  • Lee, J.S.; Pan, J.J.; Ramamoorthy, G.; Poulter, C.D.
    Structure-function studies of Artemisia tridentata farnesyl diphosphate synthase and chrysanthemyl diphosphate synthase by site-directed mutagenesis and morphogenesis (2017), J. Am. Chem. Soc., 139, 14556-14567 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information Artemisia tridentata ssp. spiciformis farnesyl diphosphate synthase (FPPase) and chrysanthemyl diphosphate synthase (CPPase) are closely related proteins. Farnesyl diphosphate synthase catalyzes the chain elongation of dimethylallyl diphosphate to farnesyl diphosphate by sequential addition of two molecules of isopentenyl diphosphate, while chrysanthemyl diphosphate synthase catalyzes chain elongation of dimethylallyl diphosphate to geranyl diphosphate along with condensation of two molecules of dimethylallyl diphosphate to give irregular isoprenoid carbon skeletons with cyclopropane, branched, and cyclobutane structures. Stepwise replacement of the helices and loops surrounding the active site of farnesyl diphosphate synthase by the corresponding regions from chrysanthemyl diphosphate synthase results in the gradual metamorphosis of the selective efficient chain elongation enzyme to a promiscuous relative that inefficiently catalyzes chain elongation and cyclopropanation/branching/cyclobutanation reactions. The initial replacements shift the preference for synthesis of farnesyl diphosphate to geranyl diphosphate, accompanied by a moderate loss in catalytic efficiency. Formation of irregular products only becomes competitive with chain elongation upon replacement of helix VIII Artemisia spiciformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 dimethylallyl diphosphate Artemisia spiciformis reaction of EC 2.5.1.67, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP diphosphate + chrysanthemyl diphosphate
-
?
2 dimethylallyl diphosphate Artemisia spiciformis reaction of EC 2.5.1.69, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP diphosphate + lavandulyl diphosphate
-
?
dimethylallyl diphosphate + isopentenyl diphosphate Artemisia spiciformis chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP diphosphate + geranyl diphosphate
-
?
dimethylallyl diphosphate + isopentenyl diphosphate Artemisia spiciformis the enzyme catalyzes the condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate to generate the C15 product (2E,6E)-farnesyl diphosphate diphosphate + geranyl diphosphate
-
?
geranyl diphosphate + isopentenyl diphosphate Artemisia spiciformis reaction of EC 2.5.1.10, the enzyme catalyzes the condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate to generate the C15 product (2E,6E)-farnesyl diphosphate diphosphate + (2E,6E)-farnesyl diphosphate
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?

Organism

Organism UniProt Comment Textmining
Artemisia spiciformis
-
-
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Artemisia spiciformis Q7XYS8
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 dimethylallyl diphosphate reaction of EC 2.5.1.67, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP Artemisia spiciformis diphosphate + chrysanthemyl diphosphate
-
?
2 dimethylallyl diphosphate reaction of EC 2.5.1.69, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP Artemisia spiciformis diphosphate + lavandulyl diphosphate
-
?
dimethylallyl diphosphate + isopentenyl diphosphate chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP Artemisia spiciformis diphosphate + geranyl diphosphate
-
?
dimethylallyl diphosphate + isopentenyl diphosphate the enzyme catalyzes the condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate to generate the C15 product (2E,6E)-farnesyl diphosphate Artemisia spiciformis diphosphate + geranyl diphosphate
-
?
geranyl diphosphate + isopentenyl diphosphate reaction of EC 2.5.1.10, the enzyme catalyzes the condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate to generate the C15 product (2E,6E)-farnesyl diphosphate Artemisia spiciformis diphosphate + (2E,6E)-farnesyl diphosphate
-
?

Synonyms

Synonyms Comment Organism
FPPase
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Artemisia spiciformis

General Information

General Information Comment Organism
evolution Artemisia tridentata chrysanthemyl diphosphate synthase is an example of an enzyme that has evolved recently from a highly specialized parent. The origins of farnesyl diphosphate synthase date back to the very beginning of cellular life, and the enzyme has perfected its ability to catalyze chain-elongation. In contrast, Artemisia tridentata chrysanthemyl diphosphate synthase has recently evolved from Artemisia tridentata diphosphate synthase, presumably by gene duplication and random mutagenesis but is still a promiscuous inefficient catalyst in comparison with farnesyl diphosphate synthase Artemisia spiciformis