BRENDA - Enzyme Database
show all sequences of 6.2.1.30

Characterization of a phenylacetate-CoA ligase from Penicillium chrysogenum

Koetsier, M.J.; Jekel, P.A.; van den Berg, M.A.; Bovenberg, R.A.; Janssen, D.B.; Biochem. J. 417, 467-476 (2008)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene phl, sequence analysis, functional expression as C-terminally His6-tagged maltose binding protein fusion in Escherichia coli, expression of His-tagged mutants
Penicillium chrysogenum
Engineering
Protein Variants
Commentary
Organism
F307A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
Penicillium chrysogenum
F335A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
Penicillium chrysogenum
additional information
construction of mutants with substrate binding pocket residues exchanged for alanine, the mutants show altered kinetics, overview
Penicillium chrysogenum
V270A
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
Penicillium chrysogenum
V370A
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
Penicillium chrysogenum
Y267A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
Penicillium chrysogenum
General Stability
General Stability
Organism
presence of 200 mM NaCl is essential for the stability of the enzyme and storage or conversions in buffer lacking NaCl resulted in rapid loss of activity
Penicillium chrysogenum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics of wild-type and mutant enzymes with diverse substrates, overview
Penicillium chrysogenum
0.001
-
myristic acid
below, pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
0.12
-
CoA
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
0.19
-
trans-cinnamic acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
0.48
-
ATP
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
0.65
-
ATP
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
0.94
-
CoA
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
2.1
-
Phenoxyacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
5.2
6.1
phenylacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
24.4
-
Butyric acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
80
-
propionic acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
dependent on, optimal at 5 mM
Penicillium chrysogenum
NaCl
stabilizes at 200 mM
Penicillium chrysogenum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
62600
-
x * 62600, recombinant enzyme, SDS-PAGE
Penicillium chrysogenum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + butyric acid + CoA
Penicillium chrysogenum
-
AMP + diphosphate + butyryl-CoA
-
-
?
ATP + phenylacetate + CoA
Penicillium chrysogenum
enzymatic activation of phenylacetic acid to phenylacetyl-CoA is an important step in the biosynthesis of the beta-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum, CoA esters of phenylacetic acid and phenoxyacetic acid act as acyl donor in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V
AMP + diphosphate + phenylacetyl-CoA
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Penicillium chrysogenum
O74725
gene phl or pclA; gene phl
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant C-terminally His6-tagged maltose binding protein fusion from Escherichia coli by nickel affinity chromatography, the MBP is cleaved off by factor Xa, imidazole is eliminated by gel filtration, recombinant His-tagged mutants
Penicillium chrysogenum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Penicillium chrysogenum
0.02
-
purified recombinant enzyme
Penicillium chrysogenum
Storage Stability
Storage Stability
Organism
-20°C, purified recombinant protein in TANG buffer, several months without significant loss of activity
Penicillium chrysogenum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + 3,4-methylenedioxycinnamic acid + CoA
high activity
690837
Penicillium chrysogenum
AMP + diphosphate + 3,4-methylenedioxycinnamoyl-CoA
-
-
-
?
ATP + 3-ethoxycinnamic acid + CoA
high activity
690837
Penicillium chrysogenum
AMP + diphosphate + 3-ethoxy-cinnamoyl-CoA
-
-
-
?
ATP + 3-methoxycinnamic acid + CoA
high activity
690837
Penicillium chrysogenum
AMP + diphosphate + 3-methoxy-cinnamoyl-CoA
-
-
-
?
ATP + butyric acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + butyryl-CoA
-
-
-
?
ATP + caproic acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + caproyl-CoA
-
-
-
?
ATP + myristic acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + myristoyl-CoA
-
-
-
?
ATP + phenoxyacetate + CoA
low activity
690837
Penicillium chrysogenum
AMP + diphosphate + phenoxyacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
enzymatic activation of phenylacetic acid to phenylacetyl-CoA is an important step in the biosynthesis of the beta-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum, CoA esters of phenylacetic acid and phenoxyacetic acid act as acyl donor in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V
690837
Penicillium chrysogenum
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + propionic acid + CoA
low activity
690837
Penicillium chrysogenum
AMP + diphosphate + propionyl-CoA
-
-
-
?
ATP + trans-4-coumaric acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + trans-4-coumaroyl-CoA
-
-
-
?
ATP + trans-cinnamic acid + CoA
1000fold higher activity compared to PAA
690837
Penicillium chrysogenum
AMP + diphosphate + trans-cinnamoyl-CoA
-
-
-
?
additional information
the enzyme also belongs to EC 6.2.1.2, substrate specificity of PCL, the more substituted compounds ferulic acid, caffeic acid and sinapic acid, which are substrates for most 4-coumarate CoA ligases, are very poor substrates for PCL. With the exception of acetic acid, all short and medium chain fatty acids tested are converted by PCL, PCL is able to activate all the side chains of these naturally occurring lactam side products, overview. Residues H265, I266, Y267, V270, F307, F335, G337, A338, G361, T369, V370, and K557 are involved in substrate binding
690837
Penicillium chrysogenum
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 62600, recombinant enzyme, SDS-PAGE
Penicillium chrysogenum
More
enzyme structure modelling of wild-type and mutant enzymes using the crystal structure of the luciferase from firefly species Luciola cruciata as template, PDB ID 2D1S
Penicillium chrysogenum
Synonyms
Synonyms
Commentary
Organism
More
cf. 6.2.1.2
Penicillium chrysogenum
PCL
-
Penicillium chrysogenum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
40
-
Penicillium chrysogenum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.3
1.9
phenylacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
1.5
-
CoA
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
1.7
-
ATP
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
9.7
-
Butyric acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
12
-
Phenoxyacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
41.2
-
trans-cinnamic acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
42.9
-
ATP
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
60.5
-
CoA
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Penicillium chrysogenum
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
dependent on
Penicillium chrysogenum
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inhibition kinetics
Penicillium chrysogenum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene phl, sequence analysis, functional expression as C-terminally His6-tagged maltose binding protein fusion in Escherichia coli, expression of His-tagged mutants
Penicillium chrysogenum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
dependent on
Penicillium chrysogenum
Engineering (protein specific)
Protein Variants
Commentary
Organism
F307A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
Penicillium chrysogenum
F335A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
Penicillium chrysogenum
additional information
construction of mutants with substrate binding pocket residues exchanged for alanine, the mutants show altered kinetics, overview
Penicillium chrysogenum
V270A
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
Penicillium chrysogenum
V370A
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
Penicillium chrysogenum
Y267A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
Penicillium chrysogenum
General Stability (protein specific)
General Stability
Organism
presence of 200 mM NaCl is essential for the stability of the enzyme and storage or conversions in buffer lacking NaCl resulted in rapid loss of activity
Penicillium chrysogenum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inhibition kinetics
Penicillium chrysogenum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics of wild-type and mutant enzymes with diverse substrates, overview
Penicillium chrysogenum
0.001
-
myristic acid
below, pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
0.12
-
CoA
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
0.19
-
trans-cinnamic acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
0.48
-
ATP
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
0.65
-
ATP
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
0.94
-
CoA
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
2.1
-
Phenoxyacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
5.2
6.1
phenylacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
24.4
-
Butyric acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
80
-
propionic acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
dependent on, optimal at 5 mM
Penicillium chrysogenum
NaCl
stabilizes at 200 mM
Penicillium chrysogenum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
62600
-
x * 62600, recombinant enzyme, SDS-PAGE
Penicillium chrysogenum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + butyric acid + CoA
Penicillium chrysogenum
-
AMP + diphosphate + butyryl-CoA
-
-
?
ATP + phenylacetate + CoA
Penicillium chrysogenum
enzymatic activation of phenylacetic acid to phenylacetyl-CoA is an important step in the biosynthesis of the beta-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum, CoA esters of phenylacetic acid and phenoxyacetic acid act as acyl donor in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V
AMP + diphosphate + phenylacetyl-CoA
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant C-terminally His6-tagged maltose binding protein fusion from Escherichia coli by nickel affinity chromatography, the MBP is cleaved off by factor Xa, imidazole is eliminated by gel filtration, recombinant His-tagged mutants
Penicillium chrysogenum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Penicillium chrysogenum
0.02
-
purified recombinant enzyme
Penicillium chrysogenum
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, purified recombinant protein in TANG buffer, several months without significant loss of activity
Penicillium chrysogenum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + 3,4-methylenedioxycinnamic acid + CoA
high activity
690837
Penicillium chrysogenum
AMP + diphosphate + 3,4-methylenedioxycinnamoyl-CoA
-
-
-
?
ATP + 3-ethoxycinnamic acid + CoA
high activity
690837
Penicillium chrysogenum
AMP + diphosphate + 3-ethoxy-cinnamoyl-CoA
-
-
-
?
ATP + 3-methoxycinnamic acid + CoA
high activity
690837
Penicillium chrysogenum
AMP + diphosphate + 3-methoxy-cinnamoyl-CoA
-
-
-
?
ATP + butyric acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + butyryl-CoA
-
-
-
?
ATP + caproic acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + caproyl-CoA
-
-
-
?
ATP + myristic acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + myristoyl-CoA
-
-
-
?
ATP + phenoxyacetate + CoA
low activity
690837
Penicillium chrysogenum
AMP + diphosphate + phenoxyacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
enzymatic activation of phenylacetic acid to phenylacetyl-CoA is an important step in the biosynthesis of the beta-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum, CoA esters of phenylacetic acid and phenoxyacetic acid act as acyl donor in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V
690837
Penicillium chrysogenum
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + propionic acid + CoA
low activity
690837
Penicillium chrysogenum
AMP + diphosphate + propionyl-CoA
-
-
-
?
ATP + trans-4-coumaric acid + CoA
-
690837
Penicillium chrysogenum
AMP + diphosphate + trans-4-coumaroyl-CoA
-
-
-
?
ATP + trans-cinnamic acid + CoA
1000fold higher activity compared to PAA
690837
Penicillium chrysogenum
AMP + diphosphate + trans-cinnamoyl-CoA
-
-
-
?
additional information
the enzyme also belongs to EC 6.2.1.2, substrate specificity of PCL, the more substituted compounds ferulic acid, caffeic acid and sinapic acid, which are substrates for most 4-coumarate CoA ligases, are very poor substrates for PCL. With the exception of acetic acid, all short and medium chain fatty acids tested are converted by PCL, PCL is able to activate all the side chains of these naturally occurring lactam side products, overview. Residues H265, I266, Y267, V270, F307, F335, G337, A338, G361, T369, V370, and K557 are involved in substrate binding
690837
Penicillium chrysogenum
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 62600, recombinant enzyme, SDS-PAGE
Penicillium chrysogenum
More
enzyme structure modelling of wild-type and mutant enzymes using the crystal structure of the luciferase from firefly species Luciola cruciata as template, PDB ID 2D1S
Penicillium chrysogenum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
40
-
Penicillium chrysogenum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.3
1.9
phenylacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
1.5
-
CoA
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
1.7
-
ATP
pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid
Penicillium chrysogenum
9.7
-
Butyric acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
12
-
Phenoxyacetate
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
41.2
-
trans-cinnamic acid
pH 8.5, 30°C, recombinant enzyme
Penicillium chrysogenum
42.9
-
ATP
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
60.5
-
CoA
pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid
Penicillium chrysogenum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Penicillium chrysogenum
Other publictions for EC 6.2.1.30
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
Synonyms
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)
727565
Yu
Cloning and characterization o ...
Penicillium chrysogenum, Penicillium chrysogenum WIS 54-1255
Folia Microbiol. (Praha)
56
246-252
2011
-
-
1
-
-
-
-
8
1
1
1
2
-
2
-
-
1
-
-
-
1
-
16
1
2
1
-
-
7
1
-
-
1
-
1
-
-
-
1
1
-
-
-
-
-
-
8
1
1
1
2
-
-
-
1
-
-
1
-
16
1
1
-
-
7
1
-
-
1
1
-
-
1
7
7
727575
Imolorhe
3-Hydroxyphenylacetic acid ind ...
Burkholderia cenocepacia, Burkholderia cenocepacia DSM 16553
Front. Cell. Infect. Microbiol.
1
14
2011
-
-
1
-
1
-
-
-
-
-
-
8
-
9
-
-
-
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
2
-
1
-
-
-
-
-
-
-
-
8
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
-
1
2
3
2
-
-
727874
Law
Defining a structural and kine ...
Burkholderia cenocepacia, Burkholderia cenocepacia DSM 16553
J. Biol. Chem.
286
15577-15585
2011
-
-
1
1
-
-
-
8
-
1
-
8
-
9
-
-
1
-
-
-
-
-
21
-
2
-
-
-
7
-
-
-
1
-
-
-
-
-
2
2
2
-
-
-
-
-
9
-
2
-
8
-
-
-
2
-
-
-
-
21
-
-
-
-
7
-
-
-
-
-
3
6
-
-
-
713830
Meijer
Peroxisomes are required for e ...
Penicillium chrysogenum, Penicillium chrysogenum NRRL1951
Appl. Environ. Microbiol.
76
5702-5709
2010
-
-
1
-
1
-
-
-
1
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
2
-
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703815
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Matching the proteome to the g ...
Penicillium chrysogenum
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2009
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705560
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Intracellular 2-keto-3-deoxy-6 ...
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Microbiology
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1
1
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706449
Gidijala
An engineered yeast efficientl ...
Penicillium chrysogenum
PLoS ONE
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6
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690837
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Characterization of a phenylac ...
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2008
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13
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11
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1
13
2
1
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8
1
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691951
Erb
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1
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1
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1
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694231
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6
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1
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671805
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Molecular cloning and function ...
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2007
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1
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661021
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6
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Induction and quantification o ...
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Aerobic metabolism of phenylac ...
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2002
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2
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648921
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Biochemical and molecular char ...
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1
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6
3
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1
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1
1
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6
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3
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3
1
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2
2
1
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3
1
1
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Schneider
Anaerobic metabolism of L-phen ...
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Minambres
Molecular cloning and expressi ...
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648916
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Purification and characterizat ...
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2
8
3
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1
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1
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1
1
2
4
1
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3
1
1
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2
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8
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3
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2
2
2
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1
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1
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1
1
2
4
1
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3
1
1
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648918
Vitovski
Phenylacetate-coenzyme A ligas ...
Achromobacter denitrificans, Acinetobacter calcoaceticus, Acinetobacter calcoaceticus EGB, Burkholderia cepacia 104P, Burkholderia cepacia 132P, Burkholderia cepacia, Burkholderia cepacia 91P, Escherichia coli, Escherichia coli ATCC 11105, Providencia rettgeri, Providencia rettgeri ATCC 31052, Pseudomonas fluorescens, Pseudomonas putida 63P, Pseudomonas putida, Pseudomonas sp., Pseudomonas sp. MT14
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16
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648915
Rodriguez-Aparacio
Fluorometric determination of ...
Pseudomonas putida
Biochim. Biophys. Acta
1073
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1991
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1
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648914
Martinez-Blanco
Purification and biochemical c ...
Pseudomonas putida
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265
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1990
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3
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10
1
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1
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6
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1
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1
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1
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13
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3
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3
1
2
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1
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2
1
10
1
1
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6
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1
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1
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648917
Kogekar
Biosynthesis of Penicillin in ...
Penicillium chrysogenum
Indian J. Biochem. Biophys.
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1982
3
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1
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1
1
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5
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1
1
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1
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3
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3
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3
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1
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1
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1
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1
1
1
5
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1
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1
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