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Literature summary for 4.2.3.46 extracted from

  • Green, S.; Friel, E.N.; Matich, A.; Beuning, L.L.; Cooney, J.M.; Rowan, D.D.; MacRae, E.
    Unusual features of a recombinant apple alpha-farnesene synthase (2006), Phytochemistry, 68, 176-188.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Malus domestica

Protein Variants

Protein Variants Comment Organism
D326A alpha-farnesene synthase, monoterpene synthase and prenyltransferase activities are lost in the mutant Malus domestica
D326A/D330A alpha-farnesene synthase, monoterpene synthase and prenyltransferase activities are lost in the mutant Malus domestica

Inhibitors

Inhibitors Comment Organism Structure
Na2MoO4 10 mM, 96% inhibition Malus domestica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
(2E,6E)-farnesyl diphosphate pH 7.5, 30°C Malus domestica

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 30-50 mM, enhances activity 5fold. Km: 3 mM. Addition of K+ reduces monoterpene synthase activity Malus domestica
Mg2+ Km: 0.7 mM Malus domestica
Mn2+ Km: 0.015 mM Malus domestica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2E,6E)-farnesyl diphosphate Malus domestica
-
(3E,6E)-alpha-farnesene + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Malus domestica Q84LB2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Malus domestica

Source Tissue

Source Tissue Comment Organism Textmining
fruit skin
-
Malus domestica
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.027
-
-
Malus domestica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate
-
Malus domestica (3E,6E)-alpha-farnesene + diphosphate
-
?
(2E,6E)-farnesyl diphosphate when farnesyl diphosphate, synthesised from 96% (E,E)-farnesol, is incubated with recombinant protein, (E,E)- and (Z,E)-alpha-farnesene are produced in a ratio of 96:4, respectively Malus domestica (3E,6E)-alpha-farnesene + beta-farnesene + diphosphate
-
?
geranyl diphosphate at 18% of the optimised rate for alpha-farnesene synthesis from farnesyl diphosphate Malus domestica linalool + (Z)-beta-ocimene + (E)-beta-ocimene + beta-myrcene
-
?
additional information although (E,E)-farnesyl diphosphate is the preferred substrate, the enzyme accepts all four isomeric forms of the farnesyl diphosphate precursor. Both isomers of beta-farnesene are also synthesised by the enzyme presumably from a specific farnesene isomer. The enzyme also produces alpha-farnesene by a reaction involving coupling of geranyl diphosphate and isoprenyl diphosphate but at less than 1% of the rate with farnesyl diphosphate Malus domestica ?
-
?

Subunits

Subunits Comment Organism
monomer
-
Malus domestica

Synonyms

Synonyms Comment Organism
alpha-farnesene synthase
-
Malus domestica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5
-
Malus domestica