Information on EC 5.5.1.8 - (+)-bornyl diphosphate synthase

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The expected taxonomic range for this enzyme is: Embryophyta

EC NUMBER
COMMENTARY hide
5.5.1.8
-
RECOMMENDED NAME
GeneOntology No.
(+)-bornyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = (+)-bornyl diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination/addition
-
-
intramolecular
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(+)-camphor biosynthesis
-
-
Biosynthesis of secondary metabolites
-
-
bornyl diphosphate biosynthesis
-
-
Metabolic pathways
-
-
Monoterpenoid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
(+)-bornyl-diphosphate lyase (decyclizing)
Requires Mg2+. The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro [3]. The reaction proceeds via isomeration of geranyl diphosphate to (3R)-linalyl diphosphate. The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (+)-bornyl diphosphate [3]. cf. EC 5.5.1.22 [(-)-bornyl diphosphate synthase].
CAS REGISTRY NUMBER
COMMENTARY hide
72668-91-8
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
bornyl diphosphate synthase is responsible for the first step in camphor biosynthesis producing bornyl diphosphate, which is subsequently hydrolyzed to borneol and then oxidized to camphor, pathway overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-(3S)-Linalyl diphosphate
(-)-(1S,4S)-Bornyl-diphosphate
show the reaction diagram
(-)-(3R)-Linalyl diphosphate
(+)-(1R,4R)-Bornyl-diphosphate
show the reaction diagram
-
-
-
-
geranyl diphosphate
(+)-bornyl diphosphate
show the reaction diagram
Geranyl diphosphate
(+)-Bornyl-diphosphate
show the reaction diagram
Geranyl diphosphate
(-)-Bornyl-diphosphate
show the reaction diagram
Geranyl diphosphate
?
show the reaction diagram
-
formation of bornyl diphosphate is the rate-limiting step in camphor biosynthesis even in immature leaf tissue
-
-
-
Neryl diphosphate
(+)-Bornyl-diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
(+)-bornyl diphosphate
show the reaction diagram
Geranyl diphosphate
?
show the reaction diagram
-
formation of bornyl diphosphate is the rate-limiting step in camphor biosynthesis even in immature leaf tissue
-
-
-
additional information
?
-
-
(di)terpene synthases seem to mediate specific reaction outcomes, at least in part, by providing electrostatic effects to counteract those exerted by the diphosphate co-product. Role for the diphosphate anion co-product in the reaction catalyzed by monoterpene cyclases, such as bornyl diphosphate synthase
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
Km: 3.5 mM; required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R)-homolinalyl diphosphate
-
i.e. 2,6-dimethyl-2-vinyl-5-heptenyl diphosphate
(3R,S)2-fluorolinalyl diphosphate
-
-
(3S)-homolinalyl diphosphate
-
i.e. 2,6-dimethyl-2-vinyl-5-heptenyl diphosphate
(E)-4-[2-Diazo-3-trifluoropropionyloxy]-3-methyl-2-buten-1-ol
-
-
2,3-Dihydrogeranyl diphosphate
-
-
2,3-Epoxygeranyl diphosphate
-
-
2-Fluorogeranyl diphosphate
-
-
2-Fluorolinalyl diphosphate
-
-
3-aza-2,3-dihydrogeranyl diphosphate
-
competitive inhibition, the aza-analog of the substrate is bound anomalously, perhaps as a consequence of the positive charge, bond distortion, or hydrogen bonding resulting from the N for C substitution, binding strutcure, overview
6,7-dihydrogeranyl diphosphate
-
-
6,7-Epoxygeranyl diphosphate
-
-
6-cyclopropylidene-(3E)-methyl-hex-2-en-1-yl diphosphate
diisopropylfluorophosphate
-
-
Dimethyl-(4-methylcyclohex-3-en-1-yl)sulfonium iodide
dimethylallyl diphosphate
-
-
diphosphate
-
-
Diphosphoric acid
-
-
Imidodiphosphonic acid
-
-
Linalyl diphosphate
-
competitive inhibition, the enantioselective synthase readily distinguishes between (3R)- and (3S)-homolinalyl diphosphates, both of which were more effective inhibitors than is 3-azageranyl diphosphate, the fluorinated analogues prove to be the most potent competitive inhibitors
Methyl-(4-methylpent-3-en-1-yl)vinyl sulfonium perchlorate
-
potency of inhibition increases with increasing substrate concentration. A combination of sulfonium analog and 0.05 mM diphosphate provides synergistic inhibition
Methylenediphosphonic acid
-
-
p-hydroxymercuribenzoate
-
-
Phosphonoformic acid
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032 - 0.007
(+)-(3S)-Linalyl diphosphate
0.0007
(-)-(3R)-Linalyl diphosphate
-
-
0.0011 - 0.0023
geranyl diphosphate
0.0037 - 0.018
neryl diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.214
(3R)-homolinalyl diphosphate
-
-
0.058
(3R,S)2-fluorolinalyl diphosphate
-
-
1.2
(3S)-homolinalyl diphosphate
-
-
0.006
2-Fluorogeranyl diphosphate
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
geranyl diphosphate and neryl diphosphate, the maximal activity with geranyl diphosphate is about 5times higher than with neryl diphosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 6.7
-
pH 5.7: about 40% of maximal activity, pH 6.7: about 35% of maximal activity, geranyl diphosphate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
each monomer contains two alpha-helical domains
additional information
-
analysis of tertiary crystal structures of bornyl diphosphate synthase, the aza moiety is ion-paired with the diphosphate, whose position is essentially invariant
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of tertiary crystal structures of bornyl diphosphate synthase complexed with diphosphate and/or aza-analogs, mimicking various carbocations of the BPS catalyzed reaction
-
hanging-drop vapor-diffusion method, structure of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with diphosphate and bornyl diphosphate, determined at 2.0 A resolution
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dye-ligand and immobilized metal ion interaction chromatography
-
mechanized techniques for the selective extraction of enzymes from plant epidermal glands
-
recombinant enzyme from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by gibberellic acids I and II in leaves, especially in young leaves
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the recombinant enzyme is similarly truncated at E50 to provide a pseudomature form devoid of the plastid transit peptide