Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.67 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
Search for more literature for 2.5.1.67

Protein Variants

Protein Variants Comment Organism
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.51
-
 dimethylallyl diphosphate pH not specified in the publication, temperature not specified in the publication Artemisia spiciformis
1.7
-
 isopentenyl diphosphate pH not specified in the publication, temperature not specified in the publication Artemisia spiciformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 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 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
-
 ?

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 dimethylallyl diphosphate
-
 Artemisia spiciformis diphosphate + chrysanthemyl diphosphate
-
 ?
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 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 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
-
 ?
isopentenyl diphosphate + dimethylallyl diphosphate
-
 Artemisia spiciformis diphosphate + geranyl diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
chrysanthemyl diphosphate synthase
-
 Artemisia spiciformis
CPPase
-
 Artemisia spiciformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.005
-
 dimethylallyl diphosphate pH not specified in the publication, temperature not specified in the publication 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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.01
-
 dimethylallyl diphosphate pH not specified in the publication, temperature not specified in the publication Artemisia spiciformis