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Information on EC 1.1.1.144 - perillyl-alcohol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.144
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.144 perillyl-alcohol dehydrogenase
IUBMB Comments
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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
ADH, dehydrogenase, perillyl alcohol, perillyl alcohol dehydrogenase, SdPOHDH, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH
dehydrogenase, perillyl alcohol
-
-
-
-
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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
limonene degradation III (to perillate), limonene degradation IV (anaerobic)
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
perillyl alcohol + NAD+
perillyl aldehyde + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
-
Substrates: 52% activity compared to cyclohexanol
Products: -
Products: -
?
(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
-
Substrates: 52% activity compared to cyclohexanol
Products: -
Products: -
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: -
Products: -
Products: -
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: e.g.: 8-hydroxyphellandrol, cumic alcohol
Products: -
Products: -
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: e.g.: 8-hydroxyphellandrol, cumic alcohol
Products: -
Products: -
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: p-ethyl benzyl alcohol, p-methyl benzyl alcohol
Products: -
Products: -
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: 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
Products: -
Products: -
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
Products: -
Products: -
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: e.g.: 8-hydroxyphellandrol, cumic alcohol
Products: -
Products: -
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: p-ethyl benzyl alcohol, p-methyl benzyl alcohol
Products: -
Products: -
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: 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
Products: -
Products: -
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
perillyl alcohol + NAD+
perillyl aldehyde + NADH + H+
Substrates: -
Products: -
Products: -
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
Products: -
Products: -
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
Substrates: catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
also active with some NAD+ analogues, e.g.: 3-acetylpyridine adenine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, deamino-NAD
additional information
-
inactive with NADP+ and with thionicotinamide adenine dinucleotide
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
o-phenanthroline
-
at concentrations higher than 3 mM and low concentration of NAD+, about 50% inhibition
p-hydroxymercuribenzoate
-
0.005 mM, complete inhibition, prevented by 10 mM glutathione
additional information
-
glucose represses the induction of the enzyme by limonene
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
-
pH 5: about 35% of activity maximum, pH 8: about 70% of activity maximum, NADH + perillyl aldehyde
6.3 - 10.5
-
at pH 6.3 and 10.5: about 10% of activity maximum, perillyl alcohol + NAD+
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ADH2_TANCI
379
0
41397
Swiss-Prot
Mitochondrion (Reliability: 4)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R50H
-
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
expression of the genes for (-)-limonene synthase (SdLS), a limonene 7-hydroxylase (SdL7H, CYP71A76), a perillyl alcohol dehydrogenase (SdPOHDH) and perillic acid O-methyltransferase (SdPAOMT) in Nicotiana benthamiana in combination with a geranyl diphosphate synthase to boost precursor formation, results in production of methylperillate
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ballal, N.R.; Bhattacharyya, P.K.; Rangachari, P.N.
Microbiological transformations of terpenes. XIV. Purification & properties of perillyl alcohol dehydrogenase
Indian J. Biochem.
5
1-6
1968
Pseudomonas sp., Pseudomonas sp. PL-
brenda
Ballal, N.R.; Bhattacharyya, P.K.; Rangachari, P.N.
Perillyl alcohol dehydrogenase from a soil pseudomonad
Biochem. Biophys. Res. Commun.
23
473-478
1966
Pseudomonas sp.
brenda
Gillooly, D.J.; Fewson, C.A.
Production of a perillyl alcohol dehydrogenase by site-directed mutagenesis of a benzyl alcohol dehydrogenase
Biotechnol. Lett.
20
325-327
1998
Acinetobacter calcoaceticus
-
brenda
Hoellrigl, V.; Hollmann, F.; Kleeb, A.C.; Buehler, K.; Schmid, A.
TADH, the thermostable alcohol dehydrogenase from Thermus sp. ATN1: a versatile new biocatalyst for organic synthesis
Appl. Microbiol. Biotechnol.
81
263-273
2008
Thermus sp., Thermus sp. ATN1
brenda
Jongedijk, E.; Mueller, S.; van Dijk, A.D.J.; Schijlen, E.; Champagne, A.; Boutry, M.; Levisson, M.; van der Krol, S.; Bouwmeester, H.; Beekwilder, J.
Novel routes towards bioplastics from plants elucidation of the methylperillate biosynthesis pathway from Salvia dorisiana trichomes
J. Exp. Bot.
71
3052-3065
2020
Salvia dorisiana (A0A6G5RUH8)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.144)
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