Information on EC 3.1.7.11 - geranyl diphosphate diphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.7.11
-
RECOMMENDED NAME
GeneOntology No.
geranyl diphosphate diphosphatase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + H2O = geraniol + diphosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
geraniol and geranial biosynthesis
-
-
Metabolic pathways
-
-
Monoterpenoid biosynthesis
-
-
secologanin and strictosidine biosynthesis
-
-
isoprenoid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphohydrolase
Isolated from Ocimum basilicum (basil) and Cinnamomum tenuipile (camphor tree). Requires Mg2+ or Mn2+. Geraniol is labelled when formed in the presence of [18O]H2O. Thus mechanism involves a geranyl cation [1]. Neryl diphosphate is hydrolysed more slowly. May be the same as EC 3.1.7.3 monoterpenyl-diphosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
139691-86-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
gene CtGES
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate + H2O
geraniol + diphosphate
show the reaction diagram
additional information
?
-
no substrate: farnesyl diphosphate. Enzyme does no display phosphatase activity
-
-
-
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
geraniol + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
dependent on, optimal at 10 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
10 mM, no residual activity
additional information
not inhibitory: sodium tungstate at 2 mM and sodium fluoride at 1 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.0585
geranyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 1
geranyl diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104.1
-
purified native enzyme, pH 8.5, 37°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
below 10% of maximal activity
6.2 - 8.2
20% of maximal activity at pH 6.2 and pH 8.2
8 - 9.5
-
70% of maximal activity at pH 8.0 and pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
calculated
5.67
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression consistently increases throughout fruit ripening
Manually annotated by BRENDA team
localization of transcripts in the internal phloem associated parenchyma
Manually annotated by BRENDA team
CtGES mRNA is localized in the oil cells of the leaves
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
stroma and stromules of plastid
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57700
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE
58600
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE
67700
x * 67700, calculated
69000
x * 69000, sequence calculation
140000
-
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 20
-
purified enzyme, 30 min, full activity remaining
37
-
purified enzyme, 30 min, 80% activity remaining
45
-
purified enzyme, 30 min, no activity remaining
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 38.3fold from leaves by two differewnt steps of anion exchange chromatography, and by gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis using a GES cDNA, isolated based on analysis of a glandular trichome expressed sequence tag database, sequence comparison, phylogenetic tree, functional expression in Escherichia coli
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DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
DNA and amino acid sequence determination and analysis, sequence comparisons
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree
-
expression in Escherichia coli
expression in Escherichia coli, Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression consistently increases throughout fruit ripening
expression is induced by methyl jasmonate
mRNA expression is induced by host-selective ACT-toxin
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information