EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
4.2.3.122 | (RS)-alpha-terpinyl diphosphate |
- |
Salvia officinalis |
limonene + diphosphate |
about 90% limonene, 10% terpinolene. Enzyme is unable to discriminate between enantiomers of alpha-terpinyl diphosphate |
? |
4.2.3.122 | geranyl diphosphate |
- |
Salvia officinalis |
(+)-alpha-pinene + diphosphate |
products are (+)-alpha-pinene, (+)-camphene, and lesser amounts of (+)-limonene, myrcene, and terpinolene. The bicyclic products of pinene and camphene are derived via the cyclization of the cisoid, anti-endo-conformers of the bound, tertiary allylic intermediate (3R)-linalyl diphosphate. A preassociation mechanism of geranyl diphosphate is suggested in which optimum folding of the terpenyl chain precedes the initial ionization step |
? |
4.2.3.122 | geranyl diphosphate |
- |
Salvia officinalis |
(+)-alpha-pinene + diphosphate |
reaction proceeds via (3R)-linalyl diphosphate and the (4R)-alpha-terpinyl cation. Products are (+)-alpha-pinene, and lesser amounts of related olefins |
? |
4.2.3.122 | geranyl diphosphate |
- |
Salvia officinalis |
(+)-beta-pinene + diphosphate |
36% (+)-alpha-pinene, 45% (+)beta-pinene |
? |
4.2.3.122 | geranyl diphosphate |
- |
Salvia officinalis |
(+)-beta-pinene + diphosphate |
products are (+)-alpha-pinene and (+)-beta-pinene |
? |
4.2.3.122 | geranyl diphosphate |
- |
Wurfbainia villosa |
beta-pinene + diphosphate |
- |
? |
4.2.3.122 | geranyl diphosphate |
stereochemistry is not specified in the publication, reaction of recombinantly expressed S-limonene sythase mutant N345A/L423A/S454A enzyme lacking the N-terminal transit peptide |
Mentha spicata |
beta-pinene + diphosphate |
- |
? |
4.2.3.122 | linalyl diphosphate |
- |
Salvia officinalis |
myrcene + diphosphate |
products are disproportionately high levels of acyclic olefins myrcene and ocimene and monocyclic olefins limonene and terpinolene. Limonene is formed via conformational foldings in addition to the cisoid, anti-endo-pattern |
? |
4.2.3.122 | more |
enzyme removes the C4-proR-hydrogen of the substrate, the C3 proton trans to the dimethyl bridge of the pinyl nucleus, with a stereoselectivity exceeding 94% in the formation of (+)-alpha-pinene |
Salvia officinalis |
? |
- |
? |
4.2.3.122 | more |
product distribution varies with deuterium substitution at C4 and C10 of substrate. Kinetic isotope effects strongly indicate multiple bicyclic olefin production through the partitioning of common carbocation intermediates |
Salvia officinalis |
? |
- |
? |