Information on EC 4.2.3.140 - cis-abienol synthase

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The expected taxonomic range for this enzyme is: Spermatophyta

EC NUMBER
COMMENTARY hide
4.2.3.140
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RECOMMENDED NAME
GeneOntology No.
cis-abienol synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(13E)-8alpha-hydroxylabd-13-en-15-yl diphosphate = cis-abienol + diphosphate
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
(13E)-8alpha-hydroxylabd-13-en-15-yl-diphosphate-lyase (cis-abienol forming)
Isolated from the plants Abies balsamea (balsam fir) [1] and Nicotiana tabacum (tobacco) [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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ectopic expression of both NtCPS2 encoding a class-II terpene synthase that synthesizes 8-hydroxy-copalyl diphosphate and NtABS, driven by a trichomespecific promoter in transgenic Nicotiana sylvestris confers Z-abienol formation to this species, which does not normally produce it
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(13E)-8alpha-hydroxylabd-13-en-15-yl diphosphate
cis-abienol + diphosphate
show the reaction diagram
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
predominantly expressed
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling based on PDB entry 3p5pA. The active site residues Asp-48, Leu617, Phe696, and Gly723 are potentially important for the specificity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinantly expressed in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D402A/D404A
monofunctional class II protein variant, complete loss of enzymatic activity with geranylgeranyl diphosphate as substrate; mutation results in complete loss of activity
D621A
monofunctional class I protein variant, mutant produces trace amounts of copalyl diphosphate plus labda-13-en-8,15-diol