Information on EC 1.1.1.323 - (+)-thujan-3-ol dehydrogenase

for references in articles please use BRENDA:EC1.1.1.323
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The expected taxonomic range for this enzyme is: Tanacetum vulgare

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EC NUMBER
COMMENTARY hide
1.1.1.323
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RECOMMENDED NAME
GeneOntology No.
(+)-thujan-3-ol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(+)-thujan-3-ol + NAD(P)+ = (+)-thujan-3-one + NAD(P)H + H+
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
(+)-thujan-3-ol:NAD(P)+ oxidoreductase
Isolated from the plant Tanacetum vulgare (tansy). NADH is preferred to NADPH.
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CAS REGISTRY NUMBER
COMMENTARY hide
75718-22-8
monoterpenol dehydrogenase, cf. EC 1.1.1.322
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
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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
(+)-thujan-3-ol + NAD(P)+
(+)-thujan-3-one + NAD(P)H + H+
show the reaction diagram
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-
-
-
?
additional information
?
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-
leaves of Tanacetum vulgare catalyse the pyridine nucleotide-dependent dehydrogenation of D-3-thujanol to D-3-thujone
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(+)-thujan-3-ol + NAD(P)+
(+)-thujan-3-one + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
leaves of Tanacetum vulgare catalyse the pyridine nucleotide-dependent dehydrogenation of D-3-thujanol to D-3-thujone
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
-
TDH shows a slight preference for NAD+ over NADP+ as cofactor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
(+)-thujan-3-ol
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pH 8.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 9.3
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50% of maximal activity at pH 6.7 and pH 9.3
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66500
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gel filtration
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the partially purified enzyme is most stable in 50 mM sodium phosphate buffer, pH 8.0
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by gel filtration
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.323)
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)