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Literature summary extracted from

  • Iijima, Y.; Gang, D.R.; Fridman, E.; Lewinsohn, E.; Pichersky, E.
    Characterization of geraniol synthase from the peltate glands of sweet basil (2004), Plant Physiol., 134, 370-379.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.7.11 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 Ocimum basilicum

Protein Variants

EC Number Protein Variants Comment Organism
3.1.7.11 additional information construction of Ser35 and Met44 truncated GES proteins showing reduced activity compared to the wild-type enzyme Ocimum basilicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.7.11 0.021
-
geranyl diphosphate pH 8.5, 37°C, wild-type enzyme Ocimum basilicum
3.1.7.11 0.029
-
geranyl diphosphate pH 8.5, 37°C, Ser35 truncated mutant Ocimum basilicum
3.1.7.11 0.03
-
geranyl diphosphate pH 8.5, 37°C, Met44-truncated mutant Ocimum basilicum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.7.11 Mn2+ required as a divalent metal cofactor for activity, activating at 0.1-1.0 mM, inhihitory above. Km value of the wild-type enzyme is 0.051 mM at pH 8.5 and 37°C Ocimum basilicum
3.1.7.11 additional information Mg2+ has no effect on the enzyme activity an cannot substitute for Mn2+ Ocimum basilicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.7.11 57700
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE Ocimum basilicum
3.1.7.11 58600
-
2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE Ocimum basilicum
3.1.7.11 140000
-
native enzyme, gel filtration Ocimum basilicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.7.11 geranyl diphosphate + H2O Ocimum basilicum
-
geraniol + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.7.11 Ocimum basilicum
-
cv. Sweet Dani
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.7.11 native enzyme 38.3fold from leaves by two differewnt steps of anion exchange chromatography, and by gel filtration Ocimum basilicum

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.7.11 geranyl diphosphate + H2O = geraniol + diphosphate the reaction mechanism of GES is similar to that of other monoterpene synthases and is different from the action of phosphatases Ocimum basilicum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.7.11 epidermis
-
Ocimum basilicum
-
3.1.7.11 leaf younger leaves, which have a higher density of epidermis, also have a higher content of monoterpenes than older leaves Ocimum basilicum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.7.11 104.1
-
purified native enzyme, pH 8.5, 37°C, wild-type enzyme Ocimum basilicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.7.11 geranyl diphosphate + H2O
-
Ocimum basilicum geraniol + diphosphate
-
?
3.1.7.11 geranyl diphosphate + H2O specific reaction Ocimum basilicum geraniol + diphosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.7.11 homodimer 2 * 57700, native enzyme, SDS-PAGE, 2 * 58600, recombinant enzyme, SDS-PAGE Ocimum basilicum

Synonyms

EC Number Synonyms Comment Organism
3.1.7.11 geraniol synthase
-
Ocimum basilicum
3.1.7.11 GES
-
Ocimum basilicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.7.11 37
-
assay at Ocimum basilicum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.7.11 4 20 purified enzyme, 30 min, full activity remaining Ocimum basilicum
3.1.7.11 37
-
purified enzyme, 30 min, 80% activity remaining Ocimum basilicum
3.1.7.11 45
-
purified enzyme, 30 min, no activity remaining Ocimum basilicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.7.11 0.6
-
geranyl diphosphate pH 8.5, 37°C, Ser35 truncated mutant Ocimum basilicum
3.1.7.11 0.8
-
geranyl diphosphate pH 8.5, 37°C, wild-type enzyme Ocimum basilicum
3.1.7.11 1
-
geranyl diphosphate pH 8.5, 37°C, Met44-truncated mutant Ocimum basilicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.7.11 8.5
-
-
Ocimum basilicum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.7.11 6 7.5 below 10% of maximal activity Ocimum basilicum
3.1.7.11 8 9.5 70% of maximal activity at pH 8.0 and pH 9.5 Ocimum basilicum