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
-
RECOMMENDED NAME
GeneOntology No.
R-linalool synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + H2O = (3R)-linalool + diphosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
linalool biosynthesis I
-
-
Monoterpenoid biosynthesis
-
-
superpathway of linalool biosynthesis
-
-
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
LeMTS1
Q1XBU5
-
R-linalool synthase
Q1XBU5
-
CAS REGISTRY NUMBER
COMMENTARY
254993-26-5
-
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
Q1XBU5
-
-
-
?
geranyl diphosphate + H2O
(3R)-linalool + diphosphate
show the reaction diagram
-
-
-
-
?
geranyl diphosphate + H2O
(3R)-linalool + diphosphate
show the reaction diagram
Q8H2B4
-
-
-
?
geranyl diphosphate + H2O
(3R)-linalool + diphosphate
show the reaction diagram
Q1XBU5
-
-
-
?
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+
Q8H2B4
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
jasmonic acid
Q1XBU5
-
additional information
Q1XBU5
expression in leaves is induced by spider mite-infestation and wounding
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
geranyl diphosphate
Q8H2B4
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
Q8H2B4
pH 6.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Q1XBU5
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Q8H2B4
half-maximal velocity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Q1XBU5
activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.22
-
isoenzyme QH1, calculated
6.6
-
isoenzyme QH5, calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of stem, isoenzyme QH5, induction by wounding
Manually annotated by BRENDA team
-
both isoenzyme QH1 and QH5
Manually annotated by BRENDA team
-
epidermis of, isoenzyme QH5, induction by wounding
Manually annotated by BRENDA team
-
both isoenzyme QH1 and QH5, induction by wounding
Manually annotated by BRENDA team
additional information
-
not: stem stele, root
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70800
Q1XBU5
predicted molecular mass
682392
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 65700, isoenzyme QH1, x * 67400, isoenzyme QH5, calculated
?
Q8H2B4
x * 70500, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Q8H2B4
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
Q8H2B4
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both isoenzyme QH1 and QH5, partial
-
recombinant protein
Q8H2B4
using Ni-agarose beads
Q1XBU5
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into the pET32-a vector for expression in Escherichia coli BL21DE3 cells
Q1XBU5
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EDTA-inactivated isoenzyme QH1, full reactivation by 10 mM Mg2+
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