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Information on EC 4.2.3.46 - alpha-farnesene synthase and Organism(s) Arabidopsis thaliana and UniProt Accession A4FVP2

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.46 alpha-farnesene synthase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: A4FVP2 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
mdafs1, tps03, tps02, alpha-farnesene synthase, afs-1, (e,e)-alpha-farnesene synthase, e,e-alpha-farnesene synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate lyase [(3E,6E)-alpha-farnesene-forming]
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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
(3E,6E)-alpha-farnesene + diphosphate
show the reaction diagram
-
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026
(2E,6E)-farnesyl diphosphate
accession Columbia, 30°C, pH not specified in the publication
0.004
(2E,6E)-farnesyl diphosphate
accession Wassilewskija, 30°C, pH not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0048
(2E,6E)-farnesyl diphosphate
accession Columbia, 30°C, pH not specified in the publication
0.0045
(2E,6E)-farnesyl diphosphate
accession Wassilewskija, 30°C, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.82
(2E,6E)-farnesyl diphosphate
accession Columbia, 30°C, pH not specified in the publication
1.12
(2E,6E)-farnesyl diphosphate
accession Wassilewskija, 30°C, pH not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform TPS03
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression occurs constitutively in floral tissues
Manually annotated by BRENDA team
expression occurs constitutively in floral tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
plastidial transit peptide of 25 amino acids, and fluoresence studies using GPF-fusion protein, accession Wassilewskija
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
differences in the relative emissions of (E)-beta-ocimene and (E,E)-alpha-farnesene from accession Wassilewskija, a high-(E)-beta-ocimene emitter, and accession Columbia, a trace-(E)-beta-ocimene emitter, are attributed to allelic variation of closely related, tandem-duplicated terpene synthase genes, TPS02 and TPS03. The Wassilewskija genome contains a functional allele of TPS02 but not of TPS03, while the opposite is the case for Columbia. Recombinant proteins of the functional Wassilewskija TPS02 and Columbia TPS03 genes both show (E)-beta-ocimene and (E,E)-alpha-farnesene synthase activities. Differential subcellular compartmentalization of the two enzymes in plastids and the cytosol is responsible for the ecotype-specific differences in (E)-beta-ocimene/(E,E)-alpha-farnesene emission
physiological function
differences in the relative emissions of (E)-beta-ocimene and (E,E)-alpha-farnesene from accession Wassilewskija, a high-(E)-beta-ocimene emitter, and accession Columbia, a trace-(E)-beta-ocimene emitter, are attributed to allelic variation of closely related, tandem-duplicated terpene synthase genes, TPS02 and TPS03. The Wassilewskija genome contains a functional allele of TPS02 but not of TPS03, while the opposite is the case for Columbia. Recombinant proteins of the functional Wassilewskija TPS02 and Columbia TPS03 genes both show (E)-beta-ocimene and (E,E)-alpha-farnesene synthase activities. Differential subcellular compartmentalization of the two enzymes in plastids and the cytosol is responsible for the ecotype-specific differences in (E)-beta-ocimene/(E,E)-alpha-farnesene emission
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPS03_ARATH
565
0
65753
Swiss-Prot
Mitochondrion (Reliability: 3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced in leaves by elicitor and insect treatment
expression is induced in leaves by elicitor and insect treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, M.; Abel, C.; Sohrabi, R.; Petri, J.; Haupt, I.; Cosimano, J.; Gershenzon, J.; Tholl, D.
Variation of herbivore-induced volatile terpenes among Arabidopsis ecotypes depends on allelic differences and subcellular targeting of two terpene synthases, TPS02 and TPS03
Plant Physiol.
153
1293-1310
2010
Arabidopsis thaliana (A4FVP2), Arabidopsis thaliana (P0CJ43)
Manually annotated by BRENDA team