EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.5.1.1 | 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 |
2.5.1.10 | 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 |
2.5.1.67 | additional information | construction of chimera between chrysanthemyl diphosphate synthase CPPase and farnesyl diphosphate synthase FPPase, EC 2.5.1.10 by sequentially replacing the loops and helices of the six-helix bundle from one enzyme with those from the other. Chain elongation is the dominant activity during the N-terminal to C-terminal metamorphosis of FPPase to CPPase, with product selectivity gradually switching from FPP to GPP, until replacement of the final alpha-helix, where upon cyclopropanation and branching activity compete with chain elongation. During the metamorphosis of CPPase to FPPase, cyclopropanation and branching activities are lost upon replacement of the first helix in the six-helix bundle. Mutations of active site residues in CPPase to the corresponding amino acids in FPPase enhance chain-elongation activity, while similar mutations in the active site of FPPase fail to significantly promote formation of significant amounts of irregular monoterpenes | Artemisia spiciformis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.67 | 0.51 | - |
dimethylallyl diphosphate | pH not specified in the publication, temperature not specified in the publication | Artemisia spiciformis | |
2.5.1.67 | 1.7 | - |
isopentenyl diphosphate | pH not specified in the publication, temperature not specified in the publication | Artemisia spiciformis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.10 | 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, reaction of EC 2.5.1.1 | diphosphate + geranyl diphosphate | - |
? | |
2.5.1.10 | geranyl 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 + (2E,6E)-farnesyl diphosphate | - |
? | |
2.5.1.67 | 2 dimethylallyl 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 + chrysanthemyl diphosphate | - |
? | |
2.5.1.67 | 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 | - |
? | |
2.5.1.67 | dimethylallyl diphosphate + isopentenyl diphosphate | Artemisia spiciformis | reaction of EC 2.5.1.1, 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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.1 | Artemisia spiciformis | - |
- |
- |
2.5.1.1 | Artemisia spiciformis | Q7XYS8 | - |
- |
2.5.1.10 | Artemisia spiciformis | Q7XYS9 | - |
- |
2.5.1.67 | Artemisia spiciformis | - |
- |
- |
2.5.1.67 | Artemisia spiciformis | Q7XYS8 | - |
- |
2.5.1.69 | Artemisia spiciformis | Q7XYS8 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.1 | 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 | - |
? | |
2.5.1.10 | 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, reaction of EC 2.5.1.1 | Artemisia spiciformis | diphosphate + geranyl diphosphate | - |
? | |
2.5.1.10 | geranyl 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 + (2E,6E)-farnesyl diphosphate | - |
? | |
2.5.1.67 | 2 dimethylallyl diphosphate | - |
Artemisia spiciformis | diphosphate + chrysanthemyl diphosphate | - |
? | |
2.5.1.67 | 2 dimethylallyl 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 + chrysanthemyl diphosphate | - |
? | |
2.5.1.67 | 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 | - |
? | |
2.5.1.67 | dimethylallyl diphosphate + isopentenyl diphosphate | reaction of EC 2.5.1.1, 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 | - |
? | |
2.5.1.67 | isopentenyl diphosphate + dimethylallyl diphosphate | - |
Artemisia spiciformis | diphosphate + geranyl diphosphate | - |
? | |
2.5.1.69 | 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 | - |
? | |
2.5.1.69 | 2 dimethylallyl 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 + lavandulyl diphosphate | - |
? | |
2.5.1.69 | dimethylallyl diphosphate + isopentenyl diphosphate | reaction of EC 2.5.1.1, 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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.1 | FPPase | - |
Artemisia spiciformis |
2.5.1.10 | FPPase | - |
Artemisia spiciformis |
2.5.1.67 | chrysanthemyl diphosphate synthase | - |
Artemisia spiciformis |
2.5.1.67 | CPPase | - |
Artemisia spiciformis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.67 | 0.005 | - |
dimethylallyl diphosphate | pH not specified in the publication, temperature not specified in the publication | Artemisia spiciformis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.5.1.1 | 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 |
2.5.1.67 | 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 |
2.5.1.69 | 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 |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.67 | 0.01 | - |
dimethylallyl diphosphate | pH not specified in the publication, temperature not specified in the publication | Artemisia spiciformis |