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Information on EC 4.2.3.55 - (S)-beta-bisabolene synthase and Organism(s) Zea mays and UniProt Accession Q1EG72

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.55 (S)-beta-bisabolene synthase
IUBMB Comments
The synthesis of (S)-beta-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps. The first step is the cyclization to (S)-beta-bisabolene. The second step is the isomerization to (S)-beta-macrocarpene (cf. EC 5.5.1.17, (S)-beta-macrocarpene synthase). The enzyme requires Mg2+ or Mn2+ for activity.
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This record set is specific for:
Zea mays
UNIPROT: Q1EG72
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Word Map
The taxonomic range for the selected organisms is: Zea mays
The enzyme appears in selected viruses and cellular organisms
Synonyms
tps11, (s)-beta-bisabolene synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene + diphosphate
show the reaction diagram
The synthesis of (S)-beta-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps. The first step is the cyclization to (S)-beta-bisabolene. The second steps is the isomerization to (S)-beta-macrocarpene (c.f. EC 5.5.1.a, (S)-beta-macrocarpene synthase). The enzyme requires Mg2+ or Mn2+ for activity.
(2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene + diphosphate
show the reaction diagram
(S)-beta-bisabolene is a stable intermediate. (S)-beta-Macrocarpene formation requires a protonation of the intermediate
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(S)-beta-bisabolene-forming]
The synthesis of (S)-beta-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps. The first step is the cyclization to (S)-beta-bisabolene. The second step is the isomerization to (S)-beta-macrocarpene (cf. EC 5.5.1.17, (S)-beta-macrocarpene synthase). The enzyme requires Mg2+ or Mn2+ for activity.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
(S)-beta-bisabolene + diphosphate
show the reaction diagram
(2Z,6E)-farnesyl diphosphate
(S)-beta-bisabolene + diphosphate
show the reaction diagram
-
The synthesis of (S)-beta-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps. The first step is the cyclization to (S)-beta-bisabolene. The second step is the isomerization to (S)-beta-macrocarpene ((S)-beta-macrocarpene synthase). Product is identified by GC-MS
-
?
(2E,6E)-farnesyl diphosphate
(S)-beta-bisabolene + diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
(S)-beta-bisabolene + diphosphate
show the reaction diagram
the enzyme may be involved in plant defense
-
-
?
(2E,6E)-farnesyl diphosphate
(S)-beta-bisabolene + diphosphate
show the reaction diagram
the enzyme may be involved in plant defense
i.e. ((4S)-1-methyl-4-(5-methyl-1-methylidenehex-4-en-1-yl)cyclohexene
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
TPS6 requires a divalent metal ion, with Mg2+ and Mn2+ being effective, optimum activity with 5 mM Mg2+ and 5 mM Mn2+. Although the Km for Mn2+ is significantly lower than for Mg2+, the enzyme is more likely to operate with a Mg2+ cofactor in planta, because the concentration of Mg2+ in plant cells is about 2 orders of magnitudes higher than Mn2+. In the presence of Mn2+, the product spectrum of TPS6 is shifted toward an increased production of (S)-beta bisabolene and a decreased production of (S)-beta-macrocarpene. KM-value for Mg2+ measured with 0.01 mM farnesyl diphosphate: 0.131 mM
Mn2+
TPS6 requires a divalent metal ion, with Mg2+ and Mn2+ being effective, optimum activity with 5 mM Mg2+ and 5 mM Mn2+. Although the Km for Mn2+ is significantly lower than for Mg2+, the enzyme is more likely to operate with a Mg2+ cofactor in planta, because the concentration of Mg2+ in plant cells is about 2 orders of magnitudes higher than Mn2+. In the presence of Mn2+, the product spectrum of TPS6 is shifted toward an increased production of (S)-beta bisabolene and a decreased production of (S)-beta-macrocarpene. KM-value for Mn2+ measured with 0.01 mM farnesyl diphosphate: 0.0234 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021
(2E,6E)-farnesyl diphosphate
30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
in presence of 5 mM Mg2+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.6
half-maximal activity at pH 6.2 and at pH 8.6, in presence of 5 mM Mg2+. Within a pH range from 5.0 to 8.0, the major product is (S)-beta-macrocarpene, but higher pH values favor the formation of (S)-beta-bisabolene
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
L. variety B73
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the enzyme is predominantly active in the roots
Manually annotated by BRENDA team
the enzyme is predominantly active in the roots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme may be involved in plant defense
physiological function
the enzyme may be involved in plant defense
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPS11_MAIZE
548
0
63938
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D526N
mutation inactivates the enzyme completely
Y522F
mutation reduces the production of (S)-beta-macrocarpene to trace amounts, the enzyme forms (S)-beta-bisabolene almost exclusively, the overall activity of the mutated enzyme is dramatically reduced
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kllner, T.G.; Schnee, C.; Li, S.; Svatos, A.; Schneider, B.; Gershenzon, J.; Degenhardt, J.
Protonation of a neutral (S)-beta-bisabolene intermediate is involved in (S)-beta-macrocarpene formation by the maize sesquiterpene synthases TPS6 and TPS11
J. Biol. Chem.
283
20779-20788
2008
Zea mays (Q1EG72), Zea mays (Q5GJ60), Zea mays
Manually annotated by BRENDA team