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show all sequences of 1.1.1.144

Production of a perillyl alcohol dehydrogenase by site-directed mutagenesis of a benzyl alcohol dehydrogenase

Gillooly, D.J.; Fewson, C.A.; Biotechnol. Lett. 20, 325-327 (1998)
No PubMed abstract available

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
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
Acinetobacter calcoaceticus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.119
-
perillyl alcohol
mutant benzyl alcohol dehydrogenase
Acinetobacter calcoaceticus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acinetobacter calcoaceticus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
perillyl alcohol + NAD+
-
285944
Acinetobacter calcoaceticus
perillyl aldehyde + NADH
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
84
-
perillyl alcohol
mutant benzyl alcohol dehydrogenase
Acinetobacter calcoaceticus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
Acinetobacter calcoaceticus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.119
-
perillyl alcohol
mutant benzyl alcohol dehydrogenase
Acinetobacter calcoaceticus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
perillyl alcohol + NAD+
-
285944
Acinetobacter calcoaceticus
perillyl aldehyde + NADH
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
84
-
perillyl alcohol
mutant benzyl alcohol dehydrogenase
Acinetobacter calcoaceticus
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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2
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1
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1
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2
-
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-
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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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-
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1
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1
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1
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1
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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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1
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1
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2
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2
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1
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2
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