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Information on EC 5.5.1.8 - (+)-bornyl diphosphate synthase
for references in articles please use BRENDA:EC5.5.1.8
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EC Tree 5 Isomerases
5.5 Intramolecular lyases
5.5.1 Intramolecular lyases (only sub-subclass identified to date)
5.5.1.8 (+)-bornyl diphosphate synthase
IUBMB Comments
Requires Mg2+. The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro . 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 . cf. EC 5.5.1.22 [(–)-bornyl diphosphate synthase].
The enzyme appears in viruses and cellular organisms
showSynonyms
bornyl diphosphate synthase, (+)-bornyl diphosphate synthase, geranyl pyrophosphate:(+)-bornyl pyrophosphate cyclase, (di)terpene synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-bornyl diphosphate synthase
(+)-Bornylpyrophosphate cyclase
-
-
-
-
(+)-BPP cyclase
-
-
-
-
(-)-BPP cyclase
-
-
-
-
bornyl diphosphate synthase
bornyl pyrophosphate synthase
-
-
-
-
bornyl pyrophosphate synthetase
-
-
-
-
BPPS
Geranyl pyrophosphate:(+)-bornyl pyrophosphate cyclase
-
-
-
-
Geranyl pyrophosphate:(-)-bornyl pyrophosphate cyclase
-
-
-
-
geranyl-diphosphate cyclase
-
-
-
-
Synthetase, bornyl pyrophosphate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = (+)-bornyl diphosphate
geranyl diphosphate is first stereospecifically isomerized to linalyl diphosphate which, following rotation about C-2-B-3 to the cisoid conformer, cyclizes from the anti-endo configuration. Neryl diphosphate cyclizes either directly or via the linalyl intermediate without the attendant rotation
-
geranyl diphosphate = (+)-bornyl diphosphate
geranyl diphosphate is first stereospecifically isomerized to linalyl diphosphate which, following rotation about C-2-B-3 to the cisoid conformer, cyclizes from the anti-endo configuration. Neryl diphosphate cyclizes either directly or via the linalyl intermediate without the attendant rotation
-
geranyl diphosphate = (+)-bornyl diphosphate
linalyl diphosphate is an intermediate
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geranyl diphosphate = (+)-bornyl diphosphate
linalyl diphosphate is an intermediate
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geranyl diphosphate = (+)-bornyl diphosphate
solely the diphosphate ester oxygen of geranyl diphosphate is involved in all the critical bonding processes in the coupled isomerization-cyclization
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geranyl diphosphate = (+)-bornyl diphosphate
solely the diphosphate ester oxygen of geranyl diphosphate is involved in all the critical bonding processes in the coupled isomerization-cyclization
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geranyl diphosphate = (+)-bornyl diphosphate
both steps of the coupled isomerization-cyclization sequence are initiated by ionization of an allylic diphosphate
-
geranyl diphosphate = (+)-bornyl diphosphate
reaction mechanism, overview
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geranyl diphosphate = (+)-bornyl diphosphate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination/addition
-
-
intramolecular
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
(+)-camphor biosynthesis, bornyl diphosphate biosynthesis
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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].
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CAS REGISTRY NUMBER
COMMENTARY
72668-91-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-(3R)-Linalyl diphosphate
(+)-(1R,4R)-Bornyl-diphosphate
-
Substrates: -
Products: -
Products: -
?
Geranyl diphosphate
?
-
Substrates: formation of bornyl diphosphate is the rate-limiting step in camphor biosynthesis even in immature leaf tissue
Products: -
Products: -
?
(+)-(3S)-Linalyl diphosphate
(-)-(1S,4S)-Bornyl-diphosphate
-
Substrates: -
Products: -
Products: -
?
(+)-(3S)-Linalyl diphosphate
(-)-(1S,4S)-Bornyl-diphosphate
-
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
-
Substrates: -
Products: the enzyme is involved in monoterpenoid cyclase catalysis, mechanism of this coupled isomerization-cyclization reaction, modeling, overview
Products: the enzyme is involved in monoterpenoid cyclase catalysis, mechanism of this coupled isomerization-cyclization reaction, modeling, overview
?
geranyl diphosphate
(+)-bornyl diphosphate
-
Substrates: cyclization
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: cyclization
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
-
Substrates: bornyl diphosphate synthase is an unusual example of a monoterpene synthase, because the diphosphate leaving group of the geranyl substrate is recaptured in the final product
Products: -
Products: -
?
Geranyl diphosphate
(+)-Bornyl-diphosphate
-
Substrates: -
Products: -
Products: -
?
Geranyl diphosphate
(+)-Bornyl-diphosphate
Substrates: -
Products: -
Products: -
?
Geranyl diphosphate
(+)-Bornyl-diphosphate
-
Substrates: -
Products: (+)-(1R,4R)-bornyl-diphosphate
Products: (+)-(1R,4R)-bornyl-diphosphate
?
Geranyl diphosphate
(+)-Bornyl-diphosphate
-
Substrates: geranyl diphosphate is preferred over neryl diphosphate
Products: -
Products: -
?
Geranyl diphosphate
(-)-Bornyl-diphosphate
-
Substrates: -
Products: -
Products: -
?
Geranyl diphosphate
(-)-Bornyl-diphosphate
-
Substrates: -
Products: (-)-(1S,4S)-bornyl-diphosphate
Products: (-)-(1S,4S)-bornyl-diphosphate
?
Neryl diphosphate
(+)-Bornyl-diphosphate
-
Substrates: -
Products: (+)-(1R,4R)-bornyl diphosphate
Products: (+)-(1R,4R)-bornyl diphosphate
?
Neryl diphosphate
(+)-Bornyl-diphosphate
-
Substrates: geranyl diphosphate is preferred over neryl diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates. The N-terminal domain has no clearly defined function, although its N-terminus caps the active site in the C-terminal domain during catalysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates. The N-terminal domain has no clearly defined function, although its N-terminus caps the active site in the C-terminal domain during catalysis
Products: -
Products: -
?
additional information
?
-
Substrates: the reaction mechanism in BPPS involves the following steps: binding of geranyl diphospahte, metal-activated ionization to yield an allylic transoid carbocation, formation of (3R)-linalyl diphosphate, rotation around the C2-C3 bond and ionization to generate a cisoid allylic cation in the reactive conformation, cyclization to form a (4R)-R-terpinyl cation, further cyclization to yield (+)-2-bornyl cation, and reincorporation of the diphosphate by the (+)-2-bornyl carbocation, to yield the final product (+)-bornyl diphosphate in ca. 75% yield
Products: -
Products: -
?
additional information
?
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Substrates: (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
Products: -
Products: -
?
additional information
?
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Substrates: hydroxyl dipole stabilization of the specific carbocation formed by initial cyclization, enabling deprotonation of this early intermediate, whereas the lack of such stabilization, i.e. in the presence of an aliphatic side chain leads to carbocation migration towards the pyrophosphate co-product, resulting in a more complex reaction. The 7-aza-7,8-dihydrolimonene analogue is clearly bound backwards to enable aza-diphosphate ion-pairing, indicating that this is the thermodynamically favored binding mode for such a carbocation. The diphosphate co-product is tightly bound and may serve as a general acid/base during terpene synthase reactions without becoming reattached itself. Consistent with such tight binding is the stereospecificity of bornyl diphosphate formation by BPS, which reattaches the bornyl cation to the same oxygen of the diphosphate involved in the original diphosphate ester bond of the GPP substrate, indicating that the diphosphate anion remains in a fixed orientation during the catalyzed reaction
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Geranyl diphosphate
?
-
Substrates: formation of bornyl diphosphate is the rate-limiting step in camphor biosynthesis even in immature leaf tissue
Products: -
Products: -
?
additional information
?
-
-
Substrates: (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
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
-
Substrates: -
Products: the enzyme is involved in monoterpenoid cyclase catalysis, mechanism of this coupled isomerization-cyclization reaction, modeling, overview
Products: the enzyme is involved in monoterpenoid cyclase catalysis, mechanism of this coupled isomerization-cyclization reaction, modeling, overview
?
geranyl diphosphate
(+)-bornyl diphosphate
-
Substrates: cyclization
Products: -
Products: -
?
geranyl diphosphate
(+)-bornyl diphosphate
Substrates: cyclization
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R)-homolinalyl diphosphate
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i.e. 2,6-dimethyl-2-vinyl-5-heptenyl diphosphate
(3S)-homolinalyl diphosphate
-
i.e. 2,6-dimethyl-2-vinyl-5-heptenyl diphosphate
3-aza-2,3-dihydrogeranyl diphosphate
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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
linalyl diphosphate
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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
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potency of inhibition increases with increasing substrate concentration. A combination of sulfonium analog and 0.05 mM diphosphate provides synergistic inhibition
6-cyclopropylidene-(3E)-methyl-hex-2-en-1-yl diphosphate
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about 50% inhibition at 0.01 mM for 20 min
6-cyclopropylidene-(3E)-methyl-hex-2-en-1-yl diphosphate
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about 50% inhibition at 0.01 mM for 20 min
Dimethyl-(4-methylcyclohex-3-en-1-yl)sulfonium iodide
-
potency of inhibition increases with increasing substrate concentration. A combination of sulfonium analog and 0.05 mM diphosphate provides synergistic inhibition
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Inhibition of monoterpene cyclases by inert analogues of geranyl diphosphate and linalyl diphosphate.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
-
geranyl diphosphate and neryl diphosphate, the maximal activity with geranyl diphosphate is about 5times higher than with neryl diphosphate
6.5 - 7
the optimum pH for the recombinant enzyme is between 6.5 and 7.0 with a dramatic loss of enzymatic activity when the pH raises up to 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7 - 6.7
-
pH 5.7: about 40% of maximal activity, pH 6.7: about 35% of maximal activity, geranyl diphosphate
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
especially in young leaves, expression pattern analysis, overview
brenda
-
the second leaf pair to emerge beyond the cotyledon from 21-day-old plants
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
physiological function
the enzyme is mainly responsible of in vivo biosynthesis of borneol/camphor in fine lavender
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BPPS_SALOF
598
0
69292
Swiss-Prot
Chloroplast (Reliability: 2)
B9S8A2_RICCO
99
0
11764
TrEMBL
other Location (Reliability: 3)
A0A185NWC6_LAVAN
602
0
70672
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the recombinant enzyme is similarly truncated at E50 to provide a pseudomature form devoid of the plastid transit peptide
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mechanized techniques for the selective extraction of enzymes from plant epidermal glands
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by gibberellic acids I and II in leaves, especially in young leaves
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lanznaster, N.; Croteau, R.
Dye-ligand immobilized metal ion interaction chromatography for the purification of enzymes of prenyl pyrophosphate metabolism
Protein Expr. Purif.
2
69-74
1991
Salvia officinalis
brenda
Wheeler, C.J.; Mihaliak, C.A.; Croteau, R.
Uncompetitive inhibition of monoterpene cyclases by an analog of the substrate geranyl pyrophosphate and inhibition of monoterpene biosynthesis in vivo by an analog of geraniol
Arch. Biochem. Biophys.
279
303-210
1990
Salvia officinalis
-
brenda
Cane, D.E.; Saito, A.; Croteau, R.; Shaskus, J.; Felton, M.
Enzymatic cyclization of geranyl pyrophosphate to bornyl pyrophosphate. Role of the pyrophosphate moiety
J. Am. Chem. Soc.
104
5831-5833
1982
Salvia officinalis
-
brenda
Croteau, R.; Shaskus, J.
Biosynthesis of monoterpenes: demonstration of a geranyl pyrophosphate:(-)-bornyl pyrophosphate cyclase in soluble enzyme preparations from tansy (Tanacetum vulgare)
Arch. Biochem. Biophys.
236
535-543
1985
Tanacetum vulgare
brenda
Croteau, R.B.; Shaskus, J.J.; Renstrom, B.; Felton, N.M.; Cane, D.E.; Saito, A.; Chang, C.
Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl and linalyl pyrophosphate to (+)- and (-)-bornyl pyrophosphate
Biochemistry
24
7077-7085
1985
Salvia officinalis, Tanacetum vulgare
brenda
Croteau, R.; Karp, F.
Biosynthesis of monoterpenes: preliminary characterization of bornyl pyrophosphate synthetase from sage (Salvia officinalis) and demonstration that geranyl pyrophosphate is the preferred substrate for cyclization
Arch. Biochem. Biophys.
198
512-522
1979
Salvia officinalis
brenda
Croteau, R.; Alonso, W.R.; Koepp, A.E.; Shim, J.H.; Cane, D.E.
Irreversible inactivation of monoterpene cyclases by a mechanism-based inhibitor
Arch. Biochem. Biophys.
307
397-404
1993
Salvia officinalis, Tanacetum vulgare
brenda
Croteau, R.; Felton, M.; Karp, F.; Kjonaas, R.
Relationship of camphor biosynthesis to leaf development in sage (Salvia officinalis)
Plant Physiol.
67
820-824
1981
Salvia officinalis
brenda
Croteau, R.; Felton, N.M.; Wheeler, C.J.
Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate
J. Biol. Chem.
260
5956-5962
1985
Salvia officinalis, Tanacetum vulgare
brenda
Wheeler, C.J.; Croteau, R.
Monoterpene cyclases: use of the noncyclizable substrate analog 6,7-dihydrogeranyl pyrophosphate to uncouple the isomerization step of the coupled isomerization-cyclization reaction
Arch. Biochem. Biophys.
246
733-742
1986
Salvia officinalis
brenda
Croteau, R.; Wheeler, C.J.; Aksela, R.; Oehlschlager, A.C.
Inhibition of monoterpene cyclases by sulfonium analogs of presumptive carbocationic intermediates of the cyclization reaction
J. Biol. Chem.
261
7257-7263
1986
Salvia officinalis
brenda
Croteau, R.; Satterwhite, D.M.; Cane, D.E.; Chang, C.C.
Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-bornyl pyrophosphate
J. Biol. Chem.
261
13438-13445
1986
Salvia officinalis, Tanacetum vulgare
brenda
Croteau, R.
Evidence for the ionization steps in monoterpene cyclization reactions using 2-fluorogeranyl and 2-fluorolinalyl pyrophosphates as substrates
Arch. Biochem. Biophys.
251
777-782
1986
Salvia officinalis
brenda
Wheeler, C.J.; Croteau, R.
Monoterpene cyclases. Stereoelectronic requirements for substrate binding and ionization
J. Biol. Chem.
262
8213-8219
1987
Salvia officinalis
brenda
Gershenzon, J.; Duffy, M.A.; Karp, F.; Croteau, R.
Mechanized techniques for the selective extraction of enzymes from plant epidermal glands
Anal. Biochem.
163
159-164
1987
Salvia officinalis, Tanacetum vulgare
brenda
Adam, K.P.; Croteau, R.
Monoterpene biosynthesis in the liverwort Conocephalum conicum: demonstration of sabinene synthase and bornyl diphosphate synthase
Phytochemistry
49
475-480
1998
Conocephalum conicum
brenda
Wheeler, C.J.; Croteau, R.
Monoterpene cyclases: physicochemical features required for pyrophosphate binding determined from inhibition by structural analogs
Arch. Biochem. Biophys.
260
250-256
1988
Salvia officinalis
brenda
Wise, M.L.; Savage, T.J.; Katahira, E.; Croteau, R.
Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase
J. Biol. Chem.
273
14891-14899
1998
Salvia officinalis (O81192)
brenda
Whittington, D.A.; Wise, M.L.; Urbansky, M.; Coates, R.M.; Croteau, R.B.; Christianson, D.W.
Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase
Proc. Natl. Acad. Sci. USA
99
15375-15380
2002
Salvia officinalis (O81192), Salvia officinalis
brenda
Karp, F.; Zhao, Y.; Santhamma, B.; Assink, B.; Coates, R.M.; Croteau, R.B.
Inhibition of monoterpene cyclases by inert analogues of geranyl diphosphate and linalyl diphosphate
Arch. Biochem. Biophys.
468
140-146
2007
Salvia officinalis
brenda
Weitman, M.; Major, D.T.
Challenges posed to bornyl diphosphate synthase: diverging reaction mechanisms in monoterpenes
J. Am. Chem. Soc.
132
6349-6360
2010
Salvia officinalis (O81192)
brenda
Zhou, K.; Peters, R.J.
Electrostatic effects on (di)terpene synthase product outcome
Chem. Commun. (Camb. )
47
4074-4080
2011
Salvia officinalis
brenda
Schmiderer, C.; Grausgruber-Groeger, S.; Grassi, P.; Steinborn, R.; Novak, J.
Influence of gibberellin and daminozide on the expression of terpene synthases and on monoterpenes in