BRENDA - Enzyme Database show
show all sequences of 1.1.1.144

Microbiological transformations of terpenes. XIV. Purification & properties of perillyl alcohol dehydrogenase

Ballal, N.R.; Bhattacharyya, P.K.; Rangachari, P.N.; Indian J. Biochem. 5, 1-6 (1968)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
dehydrogenase is induced by limonene, alpha-pinene, delta-p-menthene and to lesser extend by p-cymene
Pseudomonas sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
0.005 mM, complete inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
Cu2+
5 mM, complete inhibition, prevented by 5 mM glutathione
Pseudomonas sp.
Hg2+
0.005 mM, complete inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
iodoacetate
10 mM, 95% inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
additional information
glucose represses the induction of the enzyme by limonene
Pseudomonas sp.
NADH
competitive inhibition
Pseudomonas sp.
Ni2+
2 mM, 75% inhibition, complete reversion with 5 mM EDTA
Pseudomonas sp.
o-phenanthroline
at concentrations higher than 3 mM and low concentration of NAD+, about 50% inhibition
Pseudomonas sp.
p-hydroxymercuribenzoate
0.005 mM, complete inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
Zn2+
2 mM, 75% inhibition, complete reversion with 10 mM EDTA
Pseudomonas sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Pseudomonas sp.
0.077
-
NAD+
at pH 8.6
Pseudomonas sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
perillyl alcohol + NAD+
Pseudomonas sp.
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 aldehyde + NADH
-
Pseudomonas sp.
-
perillyl alcohol + NAD+
Pseudomonas sp. PL-strain
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 aldehyde + NADH
-
Pseudomonas sp. PL-strain
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
-
PL-strain
-
Pseudomonas sp. PL-strain
-
PL-strain
-
Purification (Commentary)
Commentary
Organism
PL-strain
Pseudomonas sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
13
-
DEAE-eluate
Pseudomonas sp.
Storage Stability
Storage Stability
Organism
-20░C, for at least 3 days, DEAE eluate
Pseudomonas sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
285942
Pseudomonas sp.
?
-
-
-
-
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
285942
Pseudomonas sp. PL-strain
?
-
-
-
-
perillyl alcohol + NAD+
e.g.: 8-hydroxyphellandrol, cumic alcohol
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
r
perillyl alcohol + NAD+
p-ethyl benzyl alcohol, p-methyl benzyl alcohol
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
r
perillyl alcohol + NAD+
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
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
r
perillyl alcohol + NAD+
catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
-
perillyl alcohol + NAD+
e.g.: 8-hydroxyphellandrol, cumic alcohol
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
r
perillyl alcohol + NAD+
p-ethyl benzyl alcohol, p-methyl benzyl alcohol
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
r
perillyl alcohol + NAD+
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
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
r
perillyl alcohol + NAD+
catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
NADH + perillyl aldehyde
Pseudomonas sp.
9.4
-
NAD+ + perillyl alcohol
Pseudomonas sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
8
pH 5: about 35% of activity maximum, pH 8: about 70% of activity maximum, NADH + perillyl aldehyde
Pseudomonas sp.
6.3
10.5
at pH 6.3 and 10.5: about 10% of activity maximum, perillyl alcohol + NAD+
Pseudomonas sp.
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
inactive with NADP+ and with thionicotinamide adenine dinucleotide
Pseudomonas sp.
NAD+
also active with some NAD+ analogues, e.g.: 3-acetylpyridine adenine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, deamino-NAD
Pseudomonas sp.
NADH
-
Pseudomonas sp.
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
dehydrogenase is induced by limonene, alpha-pinene, delta-p-menthene and to lesser extend by p-cymene
Pseudomonas sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
inactive with NADP+ and with thionicotinamide adenine dinucleotide
Pseudomonas sp.
NAD+
also active with some NAD+ analogues, e.g.: 3-acetylpyridine adenine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, deamino-NAD
Pseudomonas sp.
NADH
-
Pseudomonas sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
0.005 mM, complete inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
Cu2+
5 mM, complete inhibition, prevented by 5 mM glutathione
Pseudomonas sp.
Hg2+
0.005 mM, complete inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
iodoacetate
10 mM, 95% inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
additional information
glucose represses the induction of the enzyme by limonene
Pseudomonas sp.
NADH
competitive inhibition
Pseudomonas sp.
Ni2+
2 mM, 75% inhibition, complete reversion with 5 mM EDTA
Pseudomonas sp.
o-phenanthroline
at concentrations higher than 3 mM and low concentration of NAD+, about 50% inhibition
Pseudomonas sp.
p-hydroxymercuribenzoate
0.005 mM, complete inhibition, prevented by 10 mM glutathione
Pseudomonas sp.
Zn2+
2 mM, 75% inhibition, complete reversion with 10 mM EDTA
Pseudomonas sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Pseudomonas sp.
0.077
-
NAD+
at pH 8.6
Pseudomonas sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
perillyl alcohol + NAD+
Pseudomonas sp.
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 aldehyde + NADH
-
Pseudomonas sp.
-
perillyl alcohol + NAD+
Pseudomonas sp. PL-strain
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 aldehyde + NADH
-
Pseudomonas sp. PL-strain
-
Purification (Commentary) (protein specific)
Commentary
Organism
PL-strain
Pseudomonas sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
13
-
DEAE-eluate
Pseudomonas sp.
Storage Stability (protein specific)
Storage Stability
Organism
-20░C, for at least 3 days, DEAE eluate
Pseudomonas sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
285942
Pseudomonas sp.
?
-
-
-
-
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
285942
Pseudomonas sp. PL-strain
?
-
-
-
-
perillyl alcohol + NAD+
e.g.: 8-hydroxyphellandrol, cumic alcohol
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
r
perillyl alcohol + NAD+
p-ethyl benzyl alcohol, p-methyl benzyl alcohol
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
r
perillyl alcohol + NAD+
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
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
r
perillyl alcohol + NAD+
catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
285942
Pseudomonas sp.
perillyl aldehyde + NADH
-
285942
Pseudomonas sp.
-
perillyl alcohol + NAD+
e.g.: 8-hydroxyphellandrol, cumic alcohol
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
r
perillyl alcohol + NAD+
p-ethyl benzyl alcohol, p-methyl benzyl alcohol
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
r
perillyl alcohol + NAD+
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
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
r
perillyl alcohol + NAD+
catalyzes dehydrogenation reaction which is a part of the catabolic sequence of alpha-pinenes and beta-pinenes, limonene, DELTA1-p-methene and p-cymene
285942
Pseudomonas sp. PL-strain
perillyl aldehyde + NADH
-
285942
Pseudomonas sp. PL-strain
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
NADH + perillyl aldehyde
Pseudomonas sp.
9.4
-
NAD+ + perillyl alcohol
Pseudomonas sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
8
pH 5: about 35% of activity maximum, pH 8: about 70% of activity maximum, NADH + perillyl aldehyde
Pseudomonas sp.
6.3
10.5
at pH 6.3 and 10.5: about 10% of activity maximum, perillyl alcohol + NAD+
Pseudomonas sp.
Other publictions for EC 1.1.1.144
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [░C]
Temperature Range [░C]
Temperature Stability [░C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [░C] (protein specific)
Temperature Range [░C] (protein specific)
Temperature Stability [░C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
695811
Hoellrigl
TADH, the thermostable alcohol ...
Thermus sp., Thermus sp. ATN1
Appl. Microbiol. Biotechnol.
81
263-273
2008
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2
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1
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1
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2
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285944
Gillooly
-
Production of a perillyl alcoh ...
Acinetobacter calcoaceticus
Biotechnol. Lett.
20
325-327
1998
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1
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1
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1
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285942
Ballal
Microbiological transformation ...
Pseudomonas sp., Pseudomonas sp. PL-strain
Indian J. Biochem.
5
1-6
1968
1
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10
2
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2
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2
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1
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1
1
10
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2
2
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3
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1
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3
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10
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2
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2
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1
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1
1
10
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2
2
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285943
Ballal
Perillyl alcohol dehydrogenase ...
Pseudomonas sp.
Biochem. Biophys. Res. Commun.
23
473-478
1966
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