Information on EC 4.2.3.26 - R-linalool synthase

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The expected taxonomic range for this enzyme is: asterids

EC NUMBER
COMMENTARY
4.2.3.26
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RECOMMENDED NAME
GeneOntology No.
R-linalool synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + H2O = (3R)-linalool + diphosphate
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
linalool biosynthesis I
-
-
superpathway of linalool biosynthesis
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Monoterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [(3R)-linalool-forming]
Geranyl diphosphate cannot be replaced by isopentenyl diphosphate, dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as substrate [1]. Requires Mg2+ or Mn2+ for activity. Unlike many other monoterpene synthases, only a single product, (3R)-linalool, is formed.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R-linalool synthase
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CAS REGISTRY NUMBER
COMMENTARY
254993-26-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoenzyme QH1 and QH5
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
Swissprot
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
farnesyl diphosphate
(E)-nerolidol + diphosphate
show the reaction diagram
-
-
?
geranyl diphosphate + H2O
(3R)-linalool + diphosphate
show the reaction diagram
-
-
-
?
geranyl diphosphate + H2O
(3R)-linalool + diphosphate
show the reaction diagram
-
-
?
geranyl diphosphate + H2O
(3R)-linalool + diphosphate
show the reaction diagram
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate + H2O
(3R)-linalool + diphosphate
show the reaction diagram
Q1XBU5
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
Km-value 4.6 mM, isoenzyme QH1
Mn2+
may substitute for Mg2+
additional information
-
Mn2+ may not substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
up to 95% loss of activity, isoenzyme QH1, full reactivation by 10 mM Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
expression in leaves is induced by spider mite-infestation and wounding
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
geranyl diphosphate
pH 6.5
0.064
geranyl diphosphate
-
isoenzyme QH1, pH 7.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.24
geranyl diphosphate
Mentha x piperita subsp. citrata
Q8H2B4
pH 6.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
half-maximal velocity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.22
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isoenzyme QH1, calculated
6.6
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isoenzyme QH5, calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of stem, isoenzyme QH5, induction by wounding
Manually annotated by BRENDA team
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both isoenzyme QH1 and QH5
Manually annotated by BRENDA team
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both isoenzyme QH1 and QH5, induction by wounding
Manually annotated by BRENDA team
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epidermis of, isoenzyme QH5, induction by wounding
Manually annotated by BRENDA team
additional information
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not: stem stele, root
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70800
predicted molecular mass
682392
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 65700, isoenzyme QH1, x * 67400, isoenzyme QH5, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
sequence contains a plastidial transit peptide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of bovine serum albumine, cytochrome c, or carbonic anhydrase stabilizes with concommittant increase in both Km- and kcat-value
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both isoenzyme QH1 and QH5, partial
-
using Ni-agarose beads
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into the pET32-a vector for expression in Escherichia coli BL21DE3 cells
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EDTA-inactivated isoenzyme QH1, full reactivation by 10 mM Mg2+
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