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 hide
4.2.3.26
-
RECOMMENDED NAME
GeneOntology No.
R-linalool synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + H2O = (3R)-linalool + diphosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(3R)-linalool biosynthesis
-
-
Biosynthesis of antibiotics
-
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Biosynthesis of secondary metabolites
-
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linalool biosynthesis I
-
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Monoterpenoid biosynthesis
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
254993-26-5
-
ORGANISM
COMMENTARY hide
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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 + H2O
(3R)-linalool + diphosphate
show the reaction diagram
Q1XBU5
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Mn2+ may not substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
up to 95% loss of activity, isoenzyme QH1, full reactivation by 10 mM Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025 - 0.064
geranyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24
geranyl diphosphate
Mentha x piperita subsp. citrata
Q8H2B4
pH 6.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
half-maximal velocity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.22
-
isoenzyme QH1, calculated
6.6
-
isoenzyme QH5, calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
of stem, isoenzyme QH5, induction by wounding
Manually annotated by BRENDA team
-
both isoenzyme QH1 and QH5
Manually annotated by BRENDA team
additional information
-
not: stem stele, root
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70800
predicted molecular mass
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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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