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Information on EC 1.1.1.144 - perillyl-alcohol dehydrogenase
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1.1.1.144 perillyl-alcohol dehydrogenaseIUBMB 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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ADH, dehydrogenase, perillyl alcohol, perillyl alcohol dehydrogenase, 
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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
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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
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+
-
52% activity compared to cyclohexanol
-
-
?
(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
-
52% activity compared to cyclohexanol
-
-
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
e.g.: 8-hydroxyphellandrol, cumic alcohol
-
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
e.g.: 8-hydroxyphellandrol, cumic alcohol
-
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
p-ethyl benzyl alcohol, p-methyl benzyl alcohol
-
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
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
-
r
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
-
?
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
e.g.: 8-hydroxyphellandrol, cumic alcohol
-
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
p-ethyl benzyl alcohol, p-methyl benzyl alcohol
-
r
perillyl alcohol + NAD+
perillyl aldehyde + NADH
-
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
-
r
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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 SUBSTRATE
NATURAL 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
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
-
?
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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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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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
other Location (Reliability: 3)
A0A259U483_9FIRM
637
0
71729
TrEMBL
-
A0A259U8N5_9FIRM
633
0
70266
TrEMBL
-
A0A1U7MBW2_9FIRM
638
0
70213
TrEMBL
-
A0A086ZNB2_9BIFI
433
0
46548
TrEMBL
-
A0A0L6Z7Q9_9CLOT
474
0
53971
TrEMBL
-
A0A0L6Z6L1_9CLOT
636
0
71325
TrEMBL
-
A0A259UBX6_9FIRM
634
0
70751
TrEMBL
-
A0A1U7M748_TISCR
583
0
66612
TrEMBL
-
A0A259UE55_9FIRM
683
0
76771
TrEMBL
-
A0A259UT95_9FIRM
478
0
54204
TrEMBL
-
A0A259U8H2_9FIRM
668
0
74199
TrEMBL
-
A0A1U7MB88_9FIRM
635
0
71335
TrEMBL
-
A0A1E7RX84_BUTME
469
0
53529
TrEMBL
-
A0A151B3G4_9CLOT
431
0
49278
TrEMBL
-
A0A1E7RYM6_BUTME
463
0
53108
TrEMBL
-
A0A1U7MIS5_9FIRM
618
0
70067
TrEMBL
-
A0A151AMR8_9CLOT
592
0
67745
TrEMBL
-
A0A084FZJ5_PSEDA
342
0
36497
TrEMBL
other Location (Reliability: 2)
A3KI51_STRA7
Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
368
2
38255
TrEMBL
-
A0A259US84_9FIRM
654
0
74078
TrEMBL
-
A0A259U760_9FIRM
467
0
52259
TrEMBL
-
A0A259UDF5_9FIRM
687
0
76256
TrEMBL
-
A0A259UP01_9FIRM
691
0
78477
TrEMBL
-
A0A6J4RA22_9ACTN
150
0
16121
TrEMBL
-
A0A1U7MB55_9FIRM
627
0
69921
TrEMBL
-
A0A1U7MIU5_9FIRM
601
0
68007
TrEMBL
-
A0A259UUL8_9FIRM
474
0
54023
TrEMBL
-
A0A259U8U6_9FIRM
695
0
77743
TrEMBL
-
A0A6J4PFZ1_9ACTN
370
0
39080
TrEMBL
-
A0A1J5PPM2_9ZZZZ
168
0
18421
TrEMBL
other Location (Reliability: 3)
A0A0L6Z833_9CLOT
486
0
55403
TrEMBL
-
A0A259UGW2_9FIRM
641
0
71585
TrEMBL
-
A0A259UDW0_9FIRM
714
0
80579
TrEMBL
-
A0A6J4QJU7_9ACTN
100
0
10909
TrEMBL
-
A0A0L6Z642_9CLOT
467
0
53231
TrEMBL
-
A0A259UWD0_9FIRM
642
0
70999
TrEMBL
-
A0A151ALB6_9CLOT
446
0
51062
TrEMBL
-
A0A6J4PPS2_9ACTN
366
0
37841
TrEMBL
-
A0A087A5K8_9BIFI
440
1
47169
TrEMBL
-
A0A259UNH7_9FIRM
623
0
68840
TrEMBL
-
A0A259UN71_9FIRM
323
0
36551
TrEMBL
-
A0A1J5Q123_9ZZZZ
204
0
22453
TrEMBL
other Location (Reliability: 2)
A0A259U8Y6_9FIRM
707
0
80002
TrEMBL
-
A0A259U4X5_9FIRM
637
0
70718
TrEMBL
-
A0A1U7MCR5_9FIRM
637
0
70818
TrEMBL
-
A0A259UDI7_9FIRM
476
0
53398
TrEMBL
-
A0A0B5WZP4_BACCO
951
0
107820
TrEMBL
-
A0A259UW73_9FIRM
638
0
72020
TrEMBL
-
A0A6J4S543_9ACTN
339
0
34717
TrEMBL
-
A0A259URT8_9FIRM
600
0
67811
TrEMBL
-
A0A1U7M8V9_TISCR
435
0
50088
TrEMBL
-
A0A6J4NS10_9ACTN
366
0
38030
TrEMBL
-
A0A6J4P7I6_9ACTN
366
0
38217
TrEMBL
-
A0A6J4QYM4_9ACTN
367
0
38640
TrEMBL
-
A0A259USU3_9FIRM
622
0
67462
TrEMBL
-
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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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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
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