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EC Tree
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
Synonyms
ADH, dehydrogenase, perillyl alcohol, perillyl alcohol dehydrogenase,
more
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dehydrogenase, perillyl alcohol
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perillyl alcohol dehydrogenase
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ADH
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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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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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(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
perillyl alcohol + NAD+
perillyl aldehyde + NADH
additional information
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(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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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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perillyl alcohol + NAD+
perillyl aldehyde + NADH
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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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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NAD+
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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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additional information
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inactive with NADP+
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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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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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0.119
perillyl alcohol
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mutant benzyl alcohol dehydrogenase
additional information
additional information
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84
perillyl alcohol
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mutant benzyl alcohol dehydrogenase
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7
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NADH + perillyl aldehyde
9.4
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NAD+ + perillyl alcohol
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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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brenda
PL-strain
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brenda
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brenda
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brenda
from soil
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brenda
PL-strain
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brenda
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ADH2_TANCI
379
0
41397
Swiss-Prot
other Location (Reliability: 3 )
GEOA_CASDE
373
0
38274
Swiss-Prot
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LIHY_GEOSE
543
0
61569
Swiss-Prot
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A0A259U483_9FIRM
637
0
71729
TrEMBL
-
A0A259U8N5_9FIRM
633
0
70266
TrEMBL
-
A0A1U7MBW2_9FIRM
638
0
70213
TrEMBL
-
A0A1D7ZZ31_LIMFE
361
0
38608
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
-
A0A0J1I1L5_9FIRM
701
0
77563
TrEMBL
-
A0A0F0CK81_9CLOT
647
0
72594
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
-
A0A1A6B3W5_9CLOT
471
0
53430
TrEMBL
-
A0A0J1IC26_9FIRM
456
0
50510
TrEMBL
-
A0A0J1FFH0_9FIRM
644
0
71729
TrEMBL
-
A0A151B3G4_9CLOT
431
0
49278
TrEMBL
-
A0A1E7RYM6_BUTME
463
0
53108
TrEMBL
-
A0A1U7MIS5_9FIRM
618
0
70067
TrEMBL
-
S5ZZ60_9CLOT
471
0
53489
TrEMBL
-
A0A151AMR8_9CLOT
592
0
67745
TrEMBL
-
A0A084FZJ5_PSEDA
342
0
36497
TrEMBL
other Location (Reliability: 2 )
A0A1V4J1A7_9CLOT
574
0
64350
TrEMBL
-
A3KI51_STRA7
Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
368
2
38255
TrEMBL
-
A0A1V4IT54_9CLOT
657
0
74601
TrEMBL
-
A0A259US84_9FIRM
654
0
74078
TrEMBL
-
A0A259U760_9FIRM
467
0
52259
TrEMBL
-
A0A1S8NBP2_CLOSA
636
0
72230
TrEMBL
-
A0A0J1FBA5_9FIRM
589
0
65831
TrEMBL
-
A0A259UDF5_9FIRM
687
0
76256
TrEMBL
-
A0A259UP01_9FIRM
691
0
78477
TrEMBL
-
A0A6J4RA22_9ACTN
150
0
16121
TrEMBL
-
A0A162UF16_9CLOT
466
0
52261
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
-
A0A1D7ZZ49_LIMFE
356
0
38453
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
-
A0A1S8NJ43_CLOSA
646
0
73161
TrEMBL
-
A0A0J1FEM9_9FIRM
500
0
55862
TrEMBL
-
A0A259UDW0_9FIRM
714
0
80579
TrEMBL
-
A0A161X2B5_9CLOT
642
0
72812
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
-
A0A0F0C978_9CLOT
633
0
72687
TrEMBL
-
A0A259UNH7_9FIRM
623
0
68840
TrEMBL
-
A0A259UN71_9FIRM
323
0
36551
TrEMBL
-
A0A1J5Q123_9ZZZZ
204
0
22453
TrEMBL
other Location (Reliability: 2 )
A0A1J5P3H7_MOOTH
610
0
67937
TrEMBL
-
A0A259U8Y6_9FIRM
707
0
80002
TrEMBL
-
A0A259U4X5_9FIRM
637
0
70718
TrEMBL
-
A0A1U7MCR5_9FIRM
637
0
70818
TrEMBL
-
A0A0F0CLP0_9CLOT
636
0
70922
TrEMBL
-
A0A1F2PFT0_9FIRM
653
0
73459
TrEMBL
-
A0A0J1FH36_9FIRM
614
0
68099
TrEMBL
-
A0A1F2PME8_9FIRM
463
0
52583
TrEMBL
-
A0A161WR74_9CLOT
483
0
54662
TrEMBL
-
A0A083ZX61_9GAMM
591
1
66452
TrEMBL
-
A0A259UDI7_9FIRM
476
0
53398
TrEMBL
-
A0A0J1FKG9_9FIRM
590
0
66449
TrEMBL
-
A0A0B5WZP4_BACCO
951
0
107820
TrEMBL
-
A0A0K2YIV5_9NOCA
373
1
37894
TrEMBL
-
A0A259UW73_9FIRM
638
0
72020
TrEMBL
-
A0A1A6ANB9_9CLOT
446
0
51666
TrEMBL
-
A0A6J4S543_9ACTN
339
0
34717
TrEMBL
-
A0A0J1FA13_9FIRM
501
0
56324
TrEMBL
-
A0A087DJA4_9BIFI
436
0
46798
TrEMBL
-
A0A162S2Z3_9CLOT
350
0
39831
TrEMBL
-
A0A259URT8_9FIRM
600
0
67811
TrEMBL
-
A0A1U7M8V9_TISCR
435
0
50088
TrEMBL
-
A0A0J1IRY7_9FIRM
652
0
72919
TrEMBL
-
A0A6J4NS10_9ACTN
366
0
38030
TrEMBL
-
A0A6J4P7I6_9ACTN
366
0
38217
TrEMBL
-
A0A6J4QYM4_9ACTN
367
0
38640
TrEMBL
-
A0A1A6B3R5_9CLOT
646
0
73047
TrEMBL
-
A0A259USU3_9FIRM
622
0
67462
TrEMBL
-
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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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-20°C, for at least 3 days, DEAE eluate
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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
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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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