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Information on EC 4.2.3.113 - terpinolene synthase and Organism(s) Picea sitchensis and UniProt Accession F1CKJ1
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EC Tree
4.2.3.113 terpinolene synthaseIUBMB Comments
Requires Mg2+. Mn2+ is less effective and product ratio changes. Forms traces of other monoterpenoids.
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Word Map
- 4.2.3.113
- monoterpenes
-
cyclization
-
olefins
- officinalis
-
salvia
- beta-pinene
-
stereochemical
- cyclases
-
linalyl
-
+-alpha-pinene
- camphene
-
chemotypes
-
antipodal
-
acyclic
-
3s-linalyl
- 1,8-cineole
- myrcene
- sage
-
melaleuca
- alternifolia
-
cisoid
-
actinidia
- kiwifruit
The taxonomic range for the selected organisms is: Picea sitchensis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
aatps1, terpinolene synthase, (-)-pinene cyclase, (+)-pinene cyclase, actps1, terpene synthase1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ag9
-
-
-
-
LaLIMS_RR
-
-
-
-
PmeTPS2
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase (cyclizing, terpinolene-forming)
Requires Mg2+. Mn2+ is less effective and product ratio changes. Forms traces of other monoterpenoids.
CAS REGISTRY NUMBER
COMMENTARY
250376-08-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 geranyl diphosphate
(-)-sabinene + terpinolene + 2 diphosphate
-
wild-type produces 1.3% (+)-car-3-ene, 44.7% (-)-sabinene, 35.9% terpinolene
-
?
geranyl diphosphate
terpinolene + diphosphate
-
wild-type produces 49% (+)-car-3-ene, 8.7% (-)-sabinene, 24.7% terpinolene
-
?
2 geranyl diphosphate
(+)-car-3-ene + terpinolene + 2 diphosphate
-
wild-type produces 46.2% (+)-car-3-ene, 8.8% (-)-sabinene, 29.7% terpinolene
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0202
geranyl diphosphate
mutant A595G/F596L/L599F, 30°C, pH not specified in the publication
0.0316
geranyl diphosphate
mutant F596L, 30°C, pH not specified in the publication
0.0357
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
0.0153
geranyl diphosphate
mutant L596F, 30°C, pH not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0352
geranyl diphosphate
mutant A595G/F596L/L599F, 30°C, pH not specified in the publication
0.0825
geranyl diphosphate
mutant F596L, 30°C, pH not specified in the publication
0.545
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
0.098
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
geranyl diphosphate
mutant A595G/F596L/L599F, 30°C, pH not specified in the publication
0.0027
geranyl diphosphate
mutant F596L, 30°C, pH not specified in the publication
0.0153
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
0.0062
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SSS_PICSI
627
0
71795
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A595G
shift in product profile, mutant produces 2.4% (+)-car-3-ene, 39% (-)-sabinene, 33.3% terpinolene
A595G/F596L/L599F
shift in product profile, mutant produces 42.3% (+)-car-3-ene, 7.3% (-)-sabinene, 20.1% terpinolene
F596E
shift in product profile, mutant produces 0.5% (+)-car-3-ene, 10.2% (-)-sabinene, 5.7% terpinolene, 70.9% limonene
F596G
shift in product profile, mutant produces 10.0% (+)-car-3-ene, 11.2% (-)-sabinene, 17.3% terpinolene, 27.0% myrcene, 17.0% limonene
F596H
shift in product profile, mutant produces 2.1% (+)-car-3-ene, 46.5% (-)-sabinene, 27.1% terpinolene
F596L
shift in product profile, mutant produces 28.6% (+)-car-3-ene, 42.8% (-)-sabinene, 36.4% terpinolene
L599F
shift in product profile, mutant produces 1.5% (+)-car-3-ene, 20.2% (-)-sabinene, 32.2% terpinolene
S589A
shift in product profile, mutant produces 1.2% (+)-car-3-ene, 42.9% (-)-sabinene, 35.5% terpinolene
G595A/L596F/F599L
L596F
additional information
G595A/L596F/F599L
shift in product profile, mutant produces 1.8% (+)-car-3-ene, 23.3% (-)-sabinene, 55.2% terpinolene
G595A/L596F/F599L
shift in product profile, mutant produces 4.7% (+)-car-3-ene, 47.4% (-)-sabinene, 35.2% terpinolene
G595A/L596F/F599L
shift in product profile, mutant produces 5.4% (+)-car-3-ene, 29.0% (-)-sabinene, 26.4% terpinolene
L596F
shift in product profile, mutant produces 12.3% (+)-car-3-ene, 37.4% (-)-sabinene, 35.4% terpinolene
L596F
shift in product profile, mutant produces 5% (+)-car-3-ene, 20.9% (-)-sabinene, 53.5% terpinolene
L596F
shift in product profile, mutant produces 9.2% (+)-car-3-ene, 20.2% (-)-sabinene, 32.2% terpinolene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by or (-)-sabinene. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by or (-)-sabinene. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by or (-)-sabinene. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by or (-)-sabinene. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
additional information
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roach, C.R.; Hall, D.E.; Zerbe, P.; Bohlmann, J.
Plasticity and evolution of (+)-3-carene synthase and (-)-sabinene synthase functions of a Sitka spruce monoterpene synthase gene family associated with weevil resistance
J. Biol. Chem.
289
23859-23869
2014
Picea sitchensis (F1CKI6), Picea sitchensis (F1CKI8), Picea sitchensis (F1CKI9), Picea sitchensis (F1CKJ1)
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