Information on EC 1.1.1.322 - (-)-endo-fenchol dehydrogenase

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The expected taxonomic range for this enzyme is: Foeniculum vulgare

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EC NUMBER
COMMENTARY hide
1.1.1.322
-
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RECOMMENDED NAME
GeneOntology No.
(-)-endo-fenchol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(-)-endo-fenchol + NAD(P)+ = (+)-fenchone + NAD(P)H + H+
show the reaction diagram
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(-)-endo-fenchol:NAD(P)+ oxidoreductase
Isolated from the plant Foeniculum vulgare (fennel). NADH is slightly preferred to NADPH.
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CAS REGISTRY NUMBER
COMMENTARY hide
75718-22-8
monoterpenol dehydrogenase, cf. EC 1.1.1.323
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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
(-)-endo-fenchol + NAD(P)+
(+)-fenchone + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
leaves of Foeniculum vulgare catalysed the pyridine nudeoti-dedependen dehydrogenation of I-endo-fenchol to D-fenchone
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-
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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
(-)-endo-fenchol + NAD(P)+
(+)-fenchone + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
leaves of Foeniculum vulgare catalysed the pyridine nudeoti-dedependen dehydrogenation of I-endo-fenchol to D-fenchone
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
-
FDH 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
(-)-endo-fenchol
-
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
7 - 9.2
-
50% of maximal activity at pH 7.0 and pH 9.2
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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
89000
-
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 1.1.1.322)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)