Information on EC 4.2.3.140 - cis-abienol synthase

for references in articles please use BRENDA:EC4.2.3.140
Word Map on EC 4.2.3.140
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The enzyme appears in viruses and cellular organisms

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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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Diterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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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].
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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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
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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
(13E)-8alpha-hydroxylabd-13-en-15-yl diphosphate
cis-abienol + diphosphate
show the reaction diagram
additional information
?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
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assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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predominantly expressed
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinantly expressed in Escherichia coli
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.3.140)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)