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

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The expected taxonomic range for this enzyme is: Foeniculum vulgare

EC NUMBER
COMMENTARY hide
1.1.1.322
-
RECOMMENDED NAME
GeneOntology No.
(-)-endo-fenchol dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(-)-endo-fenchol + NAD(P)+ = (+)-fenchone + NAD(P)H + H+
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(-)-endo-fenchol:NAD(P)+ oxidoreductase
Isolated from the plant Foeniculum vulgare (fennel). NADH is slightly preferred to NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
75718-22-8
monoterpenol dehydrogenase, cf. EC 1.1.1.323
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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
-
-
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
-
FDH shows a slight preference for NAD+ over NADP+ as cofactor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
(-)-endo-fenchol
-
pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.2
-
50% of maximal activity at pH 7.0 and pH 9.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
89000
-
gel filtration
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the partially purified enzyme is most stable in 50 mM sodium phosphate buffer, pH 8.0
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by gel filtration
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