Cloned (Comment) | Organism |
---|---|
recombinant expression of truncated mutant enzymes with 30, 50, or 55 N-terminal residues deleted. The DELTA30 and DELTA50 proteins are unstable but the DELTA55 protein is successfully expressed | Lavandula x intermedia |
Crystallization (Comment) | Organism |
---|---|
purified recombinat DELTA55 LPPS enzyme mutant as dimeric apo-protein and with ligands bound, soaking of LPPS crystals with S-thiolo-dimethylallyl diphosphate and with S-thiolo-isopentenyldiphosphate, X-ray diffraction structure determination and analysis at 1.87 A resolution | Lavandula x intermedia |
Protein Variants | Comment | Organism |
---|---|---|
H78N | site-directed mutagenesis, inactive mutant | Lavandula x intermedia |
W100V | site-directed mutagenesis, the mutant shows 15% of wild-type activity | Lavandula x intermedia |
Y139F | site-directed mutagenesis, the mutant shows 62% of wild-type activity | Lavandula x intermedia |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, activates | Lavandula x intermedia |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 dimethylallyl diphosphate | Lavandula x intermedia | - |
diphosphate + lavandulyl diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lavandula x intermedia | M4QSY7 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate | the two dimethylallyl diphosphate molecules, both allylic diphosphates, condense via a so-called head-to-middle condensation to form the (C10) monterpene, lavandulyl diphosphate. The enzyme structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase, and contains an allylic site (S1) in which dimethylallyl diphosphate ionizes and a second site (S2) which houses the dimethylallyl diphosphate nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product, structure-based catalytic mechanism, overview | Lavandula x intermedia |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 dimethylallyl diphosphate | - |
Lavandula x intermedia | diphosphate + lavandulyl diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LPPS | - |
Lavandula x intermedia |
General Information | Comment | Organism |
---|---|---|
additional information | enzyme structure comparisons, ligand binding structure analysis, residue H78 is essential for catalysis, modelling, overview | Lavandula x intermedia |
additional information | the enzyme structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase, and contains an allylic site (S1) in which dimethylallyl diphosphate ionizes and a second site (S2) which houses the dimethylallyl diphosphate nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product, structure-based mechanism, overview | Lavandula x intermedia |
physiological function | the enzyme catalyzes the formation of C10 mononterpene lavandulyl diphosphate, the precursor of the fragrances (R)-lavandulol and (R)-lavandulyl acetate | Lavandula x intermedia |