Information on EC 4.2.3.110 - (+)-sabinene synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.3.110
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RECOMMENDED NAME
GeneOntology No.
(+)-sabinene synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = (+)-sabinene + diphosphate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-sabinene-forming]
Isolated from Salvia officinalis (sage). The recombinant enzyme gave 63% (+)-sabinene, 21% gamma-terpinene, and traces of other monoterpenoids. See EC 4.2.3.114 gamma-terpinene synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
141907-26-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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
(+)-sabinene + diphosphate
show the reaction diagram
geranyl diphosphate + H2O
(+)-sabinene + diphosphate
show the reaction diagram
-
63% sabinene, 21% gamma-terpinene, 7% terpinolene, 6.5% limonene, and 2.5% myrcene
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0074
geranyl diphosphate
-
pH 7.1, 31°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
epidermal gland of leaf
Manually annotated by BRENDA team
developing fruits and mature fruits
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
x * 67400, calculated, x * 62000, SDS-PAGE of recombinant protein lacking signal peptide
67400
x * 67400, calculated, x * 62000, SDS-PAGE of recombinant protein lacking signal peptide
68490
-
x * 68490, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence contains a putative signal peptide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
accumulation of alpha- and beta-thujone is not transcriptionally regulated
-
daminozide significantly decreases gene expression of the monoterpene synthases sabinene synthase, borneol synthase, and 1,8-cineole synthase
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the foliar application of gibberellic acid increases gene expression of the monoterpene synthases sabinene synthase, borneol synthase, and 1,8-cineole synthase. The amounts of alpha- and beta-thujene are not transcriptionally regulated
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
exchange of sequences corresponding by homology to the C-terminal domain including the domain spanning alpha-helix, between sabinene synthase and both bornyl diphosphate synthase and cineole synthase. Exchange of tresidues 304–377 from cineole synthase into sabinene synthase is sufficient to impart the alternative termination chemistry involving water capture to alpha-terpineol and cyclization to 1,8-cineole