Information on EC 1.1.1.144 - perillyl-alcohol dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.144
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RECOMMENDED NAME
GeneOntology No.
perillyl-alcohol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+
show the reaction diagram
oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Limonene and pinene degradation
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limonene degradation III (to perillate)
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perillyl aldehyde biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
perillyl-alcohol:NAD+ oxidoreductase
Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-73-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PL-strain
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Manually annotated by BRENDA team
strain ATN1
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Manually annotated by BRENDA team
strain ATN1
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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
(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
show the reaction diagram
perillyl alcohol + NAD+
perillyl aldehyde + NADH
show the reaction diagram
additional information
?
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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
perillyl alcohol + NAD+
perillyl aldehyde + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
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0.005 mM, complete inhibition, prevented by 10 mM glutathione
Cu2+
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5 mM, complete inhibition, prevented by 5 mM glutathione
Hg2+
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0.005 mM, complete inhibition, prevented by 10 mM glutathione
iodoacetate
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10 mM, 95% inhibition, prevented by 10 mM glutathione
NADH
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competitive inhibition
Ni2+
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2 mM, 75% inhibition, complete reversion with 5 mM EDTA
o-phenanthroline
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at concentrations higher than 3 mM and low concentration of NAD+, about 50% inhibition
p-hydroxymercuribenzoate
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0.005 mM, complete inhibition, prevented by 10 mM glutathione
Zn2+
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2 mM, 75% inhibition, complete reversion with 10 mM EDTA
additional information
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glucose represses the induction of the enzyme by limonene
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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dehydrogenase is induced by limonene, alpha-pinene, delta-p-menthene and to lesser extend by p-cymene
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.077
NAD+
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at pH 8.6
0.119
perillyl alcohol
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mutant benzyl alcohol dehydrogenase
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
84
perillyl alcohol
Acinetobacter calcoaceticus
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mutant benzyl alcohol dehydrogenase
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13
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DEAE-eluate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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NADH + perillyl aldehyde
9.4
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NAD+ + perillyl alcohol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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pH 5: about 35% of activity maximum, pH 8: about 70% of activity maximum, NADH + perillyl aldehyde
6.3 - 10.5
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at pH 6.3 and 10.5: about 10% of activity maximum, perillyl alcohol + NAD+
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, for at least 3 days, DEAE eluate
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from soil
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PL-strain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R50H
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mutation of active site arginine to a histidine can switch substrate specificity of the enzyme benzyl alcohol dehydrogenase (EC 1.1.1.90) so that it has a very much greater preference for perillyl alcohol than for benzyl alcohol