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Enzyme Nomenclature
Information on EC 1.1.1.144 - perillyl-alcohol dehydrogenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.144
-
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RECOMMENDED NAME
GeneOntology No.
perillyl-alcohol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+
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
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37250-73-0
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
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52% activity compared to cyclohexanol
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?
(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
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52% activity compared to cyclohexanol
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?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
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e.g.: 8-hydroxyphellandrol, cumic alcohol
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perillyl alcohol + NAD+
perillyl aldehyde + NADH
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e.g.: 8-hydroxyphellandrol, cumic alcohol
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r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
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p-ethyl benzyl alcohol, p-methyl benzyl alcohol
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r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
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rate of the reverse reaction is about 20% of the rate of the forward reaction, 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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r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
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catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
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perillyl alcohol + NAD+
perillyl aldehyde + NADH
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e.g.: 8-hydroxyphellandrol, cumic alcohol
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r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
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p-ethyl benzyl alcohol, p-methyl benzyl alcohol
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r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
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rate of the reverse reaction is about 20% of the rate of the forward reaction, 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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r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
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catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
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additional information
?
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no substrates are p-menthan-7-ol, DELTA1-p-menthen-10-ol, DELTA8-menthen-10-ol, p-menthan-10-ol, myrtenol, isoborneol, borneol, cyclohexenol, o-menthyl benzyl alcohol, phthalyl alcohol, salicylic alcohol, 7-methyl cumic alcohol, ethanol, methanol
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additional information
?
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no substrates are p-menthan-7-ol, DELTA1-p-menthen-10-ol, DELTA8-menthen-10-ol, p-menthan-10-ol, myrtenol, isoborneol, borneol, cyclohexenol, o-menthyl benzyl alcohol, phthalyl alcohol, salicylic alcohol, 7-methyl cumic alcohol, ethanol, methanol
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additional information
?
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no substrates are p-menthan-7-ol, DELTA1-p-menthen-10-ol, DELTA8-menthen-10-ol, p-menthan-10-ol, myrtenol, isoborneol, borneol, cyclohexenol, o-menthyl benzyl alcohol, phthalyl alcohol, salicylic alcohol, 7-methyl cumic alcohol, ethanol, methanol
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
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perillyl alcohol + NAD+
perillyl aldehyde + NADH
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catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
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also active with some NAD+ analogues, e.g.: 3-acetylpyridine adenine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, deamino-NAD
additional information
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inactive with NADP+ and with thionicotinamide adenine dinucleotide
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
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glucose represses the induction of the enzyme by limonene
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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+
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.144)
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