Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is wound-inducible | Abies grandis |
Cloned (Comment) | Organism |
---|---|
gene ag1, cloning from a wound-induced stem-cDNA library, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, functional expression in Escherichia coli strain XL1-Blue | Abies grandis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | activates, but Mn2+ at concentrations higher than 1 mM results in a decline of activity with either substrate | Abies grandis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KCl | only weakly influences GDP conversion with the ag1 enzyme causing a 2fold activation at 100 mM KCl, but the monovalent cation has no effect with FDP as substrate | Abies grandis | |
Mg2+ | activates, saturation with Mg2+ is reached at 5 mM, and no apparent inhibition of catalysis occurs up to 100 mM | Abies grandis | |
Mn2+ | activates, but Mn2+ at concentrations higher than 1 mM results in a decline of activity with either substrate | Abies grandis | |
additional information | the activity of recombinant ag1 requires a divalent cation cofactor, Mg2+ or Mn2+, which is employed to neutralize the negative charge of the diphosphate leaving group in the substrate ionization step of the reaction sequence. Mg2+ is more efficient in catalysis than is Mn2+. With GDP as substrate, however, Mn2+ at 0.5 mM yields a 4fold higher rate of monoterpene synthase activity compared to Mg2+ at concentrations up to 50 mM | Abies grandis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
93776 | - |
x * 93776, sequence calculation | Abies grandis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate | Abies grandis | - |
(E)-alpha-bisabolene + diphosphate | (E)-alpha-bisabolene is the precursor in Abies species of todomatuic acid, juvabione, and related insect juvenile hormone mimics, overview | ? | |
additional information | Abies grandis | induced (E)-alpha-bisabolene biosynthesis constitutes part of a defense response targeted to insect herbivores, and possibly fungal pathogens, that is distinct from induced oleoresin monoterpene production | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Abies grandis | O81086 | gene ag1 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(2E,6E)-farnesyl diphosphate = (E)-alpha-bisabolene + diphosphate | electrophilic reaction mechanism | Abies grandis |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate | - |
Abies grandis | (E)-alpha-bisabolene + diphosphate | (E)-alpha-bisabolene is the precursor in Abies species of todomatuic acid, juvabione, and related insect juvenile hormone mimics, overview | ? | |
(2E,6E)-farnesyl diphosphate | the recombinant enzymes is substrate-specific and produces (E)-alpha-bisabolene as sole product | Abies grandis | (E)-alpha-bisabolene + diphosphate | - |
? | |
additional information | induced (E)-alpha-bisabolene biosynthesis constitutes part of a defense response targeted to insect herbivores, and possibly fungal pathogens, that is distinct from induced oleoresin monoterpene production | Abies grandis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 93776, sequence calculation | Abies grandis |
Synonyms | Comment | Organism |
---|---|---|
(E)-alpha-bisabolene synthase | - |
Abies grandis |
More | the enzyme belongs to the terpenoid synthases, subgroup sesquiterpene synthases | Abies grandis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Abies grandis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Abies grandis | sequence calculation | - |
5.03 |