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Information on EC 4.2.3.69 - (+)-alpha-barbatene synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q4KSH9

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.69 (+)-alpha-barbatene synthase
IUBMB Comments
The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% alpha-barbatene, 17.8% thujopsene (cf. EC 4.2.3.79, thujopsene synthase) and 9.9% beta-chamigrene (cf. EC 4.2.3.78, beta-chamigrene synthase) plus traces of other sesquiterpenoids .
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q4KSH9
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
at5g44630, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-alpha-barbatene-forming]
The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% alpha-barbatene, 17.8% thujopsene (cf. EC 4.2.3.79, thujopsene synthase) and 9.9% beta-chamigrene (cf. EC 4.2.3.78, beta-chamigrene synthase) [1] plus traces of other sesquiterpenoids [2].
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
(+)-alpha-barbatene + diphosphate
show the reaction diagram
-
further products are: (+)-thujopsene + isobazzanene + (+)-beta-barbatene + E -beta-farnesene + beta-acoradiene + (+)-beta-chamigrene + alpha-zingiberene + alpha-cuprenene + alpha-chamigrene + (–)-cuparene + (–)-?-bisabolene + beta-sesquiphellandrene + delta-cuprenene
-
?
farnesyl diphosphate
alpha-barbatene + diphosphate
show the reaction diagram
-
main products, 27.3% alpha-barbatene, 17.8% thujopsene, and 9.9% b-chamigrene, plus 13 minor products
-
?
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
farnesyl diphosphate
alpha-barbatene + diphosphate
show the reaction diagram
-
main products, 27.3% alpha-barbatene, 17.8% thujopsene, and 9.9% b-chamigrene, plus 13 minor products
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
1 mM, complete loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
(2E,6E)-farnesyl diphosphate
pH not specified in the publication, temperature not specified in the publication
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
intrafloral nectaries, exclusive expression in flower
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the volatile blend from flowers of an T-DNA insertion line contains only group A sesquiterpenes, including (E)-beta-caryophyllene, in similar ratios as the wild type, but none of the group B sesquiterpene compounds
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BARS_ARATH
557
0
64909
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64908
x * 64908, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 64908, calculated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Petunia hybrida infiltrated with Agrobacterium tumefaciens harboring the enzyme gene
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
method for the recovery of full-length cDNAs from predicted terpene synthase genes containing introns. The approach utilizes Agrobacterium-mediated transient expression coupled with a reverse transcription-polydeoxyribonucleotide chain reaction assay to facilitate expression cloning of processed transcripts. Subsequent expression of intronless cDNAs in a suitable prokaryotic host provides for direct functional testing of the encoded gene product
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, S.; Schoenbeck, M.A.; Greenhagen, B.T.; Takahashi, S.; Lee, S.; Coates, R.M.; Chappell, J.
Surrogate splicing for functional analysis of sesquiterpene synthase genes
Plant Physiol.
138
1322-1333
2005
Arabidopsis thaliana (Q4KSH9)
Manually annotated by BRENDA team
Tholl, D.; Chen, F.; Petri, J.; Gershenzon, J.; Pichersky, E.
Two sesquiterpene synthases are responsible for the complex mixture of sesquiterpenes emitted from Arabidopsis flowers
Plant J.
42
757-771
2005
Arabidopsis thaliana (Q4KSH9), Arabidopsis thaliana
Manually annotated by BRENDA team