Information on EC 6.2.1.30 - phenylacetate-CoA ligase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
6.2.1.30
-
RECOMMENDED NAME
GeneOntology No.
phenylacetate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + phenylacetate + CoA = AMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
thioester formation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-phenylalanine degradation IV (mammalian, via side chain)
-
-
Microbial metabolism in diverse environments
-
-
penicillin G and penicillin V biosynthesis
-
-
phenylacetate degradation I (aerobic)
-
-
phenylacetate degradation II (anaerobic)
-
-
Phenylalanine metabolism
-
-
phenylacetate degradation (aerobic)
-
-
SYSTEMATIC NAME
IUBMB Comments
phenylacetate:CoA ligase (AMP-forming)
Also acts, more slowly, on acetate, propanoate and butanoate, but not on hydroxy derivatives of phenylacetate and related compounds.
CAS REGISTRY NUMBER
COMMENTARY hide
57219-71-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain EGB
-
-
Manually annotated by BRENDA team
strain EGB
-
-
Manually annotated by BRENDA team
; strain 104P; strain 132P; strain 91P
-
-
Manually annotated by BRENDA team
strain 104P
-
-
Manually annotated by BRENDA team
strain 132P
-
-
Manually annotated by BRENDA team
strain 91P
-
-
Manually annotated by BRENDA team
ATCC11105
-
-
Manually annotated by BRENDA team
ATCC11105
-
-
Manually annotated by BRENDA team
strain AS-P-78
-
-
Manually annotated by BRENDA team
; a strain with increased penicillin production rate
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ATCC31052
-
-
Manually annotated by BRENDA team
ATCC31052
-
-
Manually annotated by BRENDA team
strain ST
-
-
Manually annotated by BRENDA team
strain 63P
-
-
Manually annotated by BRENDA team
strain KB 740
-
-
Manually annotated by BRENDA team
strain MT14
-
-
Manually annotated by BRENDA team
strain Y2 and diverse derivatives, overview, genes paaF1, paaF2, and paaF3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain HB27, DSMZ 7093, gene paaK
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phenylacetate + CoA
?
show the reaction diagram
-
28% of the activity with ATP
-
-
?
ATP + 3,4-methylenedioxycinnamic acid + CoA
AMP + diphosphate + 3,4-methylenedioxycinnamoyl-CoA
show the reaction diagram
high activity
-
-
?
ATP + 3-chlorophenylacetate + CoA
AMP + diphosphate + 3-chlorophenylacetyl-CoA
show the reaction diagram
ATP + 3-ethoxycinnamic acid + CoA
AMP + diphosphate + 3-ethoxy-cinnamoyl-CoA
show the reaction diagram
high activity
-
-
?
ATP + 3-hydroxyphenylacetate + CoA
AMP + diphosphate + 3-hydroxyphenylacetyl-CoA
show the reaction diagram
ATP + 3-methoxycinnamic acid + CoA
AMP + diphosphate + 3-methoxy-cinnamoyl-CoA
show the reaction diagram
high activity
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaryl-CoA
show the reaction diagram
reaction of EC 6.2.1.12
-
-
?
ATP + 4-hydroxyphenylacetate + CoA
AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
show the reaction diagram
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
show the reaction diagram
-
85% of the activity with phenylacetate
-
-
?
ATP + butanoate + CoA
AMP + diphosphate + butanoyl-CoA
show the reaction diagram
-
19% of the activity with phenylacetate
-
-
?
ATP + butyric acid + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
?
ATP + caprate + CoA
AMP + diphosphate + capryl-CoA
show the reaction diagram
-
-
-
?
ATP + caproate + CoA
AMP + diphosphate + caproyl-CoA
show the reaction diagram
best substrate
-
-
?
ATP + caproic acid + CoA
AMP + diphosphate + caproyl-CoA
show the reaction diagram
-
-
-
?
ATP + caprylate + CoA
AMP + diphosphate + caprylyl-CoA
show the reaction diagram
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
ATP + myristic acid + CoA
AMP + diphosphate + myristoyl-CoA
show the reaction diagram
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmityl-CoA
show the reaction diagram
low activity, reaction of EC 6.2.1.3
-
-
?
ATP + phenoxyacetate + CoA
AMP + diphosphate + phenoxyacetyl-CoA
show the reaction diagram
ATP + phenoxyacetic acid + CoA
AMP + phenoxyacetyl-CoA + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + phenoxyacetic acid + hydroxylamine
AMP + phenylacetoxyhydroxamate + diphosphate
show the reaction diagram
-
-
-
?
ATP + phenylacetate + CoA
?
show the reaction diagram
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
ATP + phenylacetic acid + hydroxylamine
AMP + phenylacetylhydroxamate + diphosphate
show the reaction diagram
-
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
show the reaction diagram
-
47% of the activity with phenylacetate
-
-
?
ATP + propionic acid + CoA
AMP + diphosphate + propionyl-CoA
show the reaction diagram
low activity
-
-
?
ATP + stearate + CoA
AMP + diphosphate + stearyl-CoA
show the reaction diagram
very low activity, reaction of EC 6.2.1.3
-
-
?
ATP + trans-4-coumaric acid + CoA
AMP + diphosphate + trans-4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + trans-cinnamic acid + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
show the reaction diagram
1000fold higher activity compared to PAA
-
-
?
CTP + phenylacetate + CoA
CMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
-
2.8% of the activity with ATP
-
-
?
UTP + phenylacetate + CoA
UMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
-
2.5% of the activity with ATP
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-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + butyric acid + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
O74725
-
-
-
?
ATP + phenylacetate + CoA
?
show the reaction diagram
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
stabilizes at 200 mM
additional information
-
enzyme does not contain metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
1 mM, 92% inhibition
Decanoic acid
-
-
Fe2+
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0.01 mM, complete inhibition
Hg2+
-
1 mM, 95% inhibition
iodoacetamide
Mo5+
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2 mM, 80% inhibition
n-octylglucoside
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-
Nonanoic acid
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-
Nonidet P-40
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-
Octanoic acid
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-
p-chloromercuribenzoate
p-hydroxymercuribenzoate
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-
Tween 100
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-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
0.01 mM, 100% stimulation
dithiothreitol
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0.01 mM, 80% stimulation
GSH
-
0.01 mM, 60% stimulation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 1.5
3-Chlorophenylacetate
0.17 - 0.87
3-hydroxyphenylacetate
0.54
4-hydroxyphenylacetate
-
pH and temperature not specified in the publication
0.006 - 9.7
ATP
24.4
Butyric acid
pH 8.5, 30°C, recombinant enzyme
0.07
caprate
recombinant enzyme, pH 7.5, 30°C
0.026
caproate
recombinant enzyme, pH 7.5, 30°C
0.046
caprylate
recombinant enzyme, pH 7.5, 30°C
0.03 - 1
CoA
0.001
myristic acid
below, pH 8.5, 30°C, recombinant enzyme
0.092
palmitate
recombinant enzyme, pH 7.5, 30°C
0.257 - 2.1
Phenoxyacetate
0.0029 - 16.5
phenylacetate
80
propionic acid
pH 8.5, 30°C, recombinant enzyme
0.841
stearate
recombinant enzyme, pH 7.5, 30°C
0.19
trans-cinnamic acid
pH 8.5, 30°C, recombinant enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 1.67
3-Chlorophenylacetate
1.83 - 2.67
3-hydroxyphenylacetate
1.17
4-hydroxyphenylacetate
Burkholderia cenocepacia
-
pH and temperature not specified in the publication
1.7 - 42.9
ATP
9.7
Butyric acid
Penicillium chrysogenum
O74725
pH 8.5, 30°C, recombinant enzyme
0.102
caprate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
0.076
caproate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
0.073
caprylate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
1.5 - 60.5
CoA
0.026
palmitate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
0.063 - 12
Phenoxyacetate
0.099 - 40
phenylacetate
0.062
stearate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
41.2
trans-cinnamic acid
Penicillium chrysogenum
O74725
pH 8.5, 30°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.455
caprate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
7402
2.917
caproate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
3991
1.575
caprylate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
4089
0.283
palmitate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
517
0.247
Phenoxyacetate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
9349
0.124
phenylacetate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
776
0.074
stearate
Penicillium chrysogenum
D3GE78
recombinant enzyme, pH 7.5, 30°C
1689
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000076
-
maximal specific activity in growing cultures
0.00013
purified recombinant enzyme, pH 7.5, 30°C
0.001
below, glycerol-grown cells
0.018
phenylacetate-grown cells
0.02
purified recombinant enzyme
0.025
phenylalanine-grown cells
24
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
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-
8.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
pH 9: 55% of maximal activity, pH 9.0: 50% of maximal activity
8.5 - 9
-
pH 8.5: activity maximum, pH 9.0: 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32 - 42
-
32°C: about 40% of maximal activity, 42°C: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
isoelectric focusing
6.1
-
isoelectric focusing
7.66
sequence calculation
8.34
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
the enzyme has a peroxisomal targeting signal on its C-terminal
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
gel filtration
48750
-
x * 48750, calculation from nucleotide sequence
51000
2 * 51000, recombinant enzyme, SDS-PAGE
61635
x * 61635, sequence calculation
62600
x * 62600, recombinant enzyme, SDS-PAGE
62638
x * 62638, calculated from sequence
64000
x * 64000, SDS-PAGE
110000
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 51000, recombinant enzyme, SDS-PAGE
monomer
additional information
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adenylated phenylacetate intermediate complex of purified recombinant His-tagged PaaK2, sitting drop vapor diffusion method, 12 mg/ml protein in 20 mM HEPES, pH 8.3, 10 mM NaCl, 3 mM 2-mercaptoethanol, 2% glycerol, 3 mM MgCl2, and 3 mM ATP, is mixed with 17% w/v PEG 6000, 0.1 M HEPES, pH 7.5, 0.1 M KCl, and 2.5% glycerol, X-ray diffraction structure determination and analysis at 1.90 A resolution; purified recombinant His-tagged selenomethionine derivative of PaaK1 in complex with ATP and adenylated phenylacetate intermediate complex of purified recombinant His-tagged PaaK1, sitting drop vapor diffusion method, 12 mg/ml protein in 20 mM HEPES, pH 8.3, 10 mM NaCl, 3 mM 2-mercaptoethanol, 2% glycerol, 3 mM MgCl2, and 3 mM ATP, is mixed with 20-25% PEG 3350, 200 mM potassium thiocyanate, and 5% glycerol. Crystals of PaaK1 are grown from 10% w/v PEG 8000, 0.1 M HEPES, pH 7.5, and 8.0% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 1.6 A and 1.92 A resolution, respectively
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
45 min stable, about 15% loss of activity after 60 min
25
-
30 min, about 20% loss of activity
30
-
60 min, about 40% loss of activity
37
-
60 min, about 75% loss of activity
45
-
15 min, about 90% loss of activity
additional information
-
glycerol, 20% v/v, ATP, MgCl2 or phenylacetic acid protects against thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
enzyme is rather labile and requires the presence of glycerol and/or phenylacetate for stabilization
-
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
purified enzyme is sensitive to repeated freezing
repeated freezing and thawing inactivates
-
sucrose stabilizes
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
insensitive to oxygen
-
648916
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or -70°C, 70% loss of activity after 1 week
-
-20°C, 10% glycerol, activity is retained for 2 months without remarkable loss of activity
-
-20°C, crude enzyme is stable in presence of glycerol for 2-3 weeks, more than 50% loss of activity of the purified enzyme
-
-20°C, purified recombinant protein in TANG buffer, several months without significant loss of activity
0°C, 24 h, very little activity retained, sucrose and 2-mercaptoethanol stabilize
-
4°C, 10% glycerol, 65% of the activity is recovered after 72 h
-
4°C, 90% loss of activity after 1 day without glycerol, plus 10% glycerol, half-life: 2 days, plus 5 mM phenylacetate, half-life: 1 week, plus 35% glycerol, half-life: 2 weeks
-
4°C, purified recombinant enzyme, 72 h no loss of activity, in the presence of 10% glycerol stable for up to 3 weeks
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
recombinant C-terminally His8-tagged enzyme from Escherichia coli strain BL21 (DE3)-RP by nickel affinity chromatography
recombinant His-tagged isozyme PaaK1 from Escherichia coli strain BL21Star(DE3) and selenomethionine-labeled His-tagged PaaK1 from Escherichia coli strain 834(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography; recombinant His-tagged isozyme PaaK2 from Escherichia coli strain BL21Star(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography
-
recombinant His6-tagged enzyme from Escherichia coli
strain KB 740
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Penicillium chrysogenum
-
for the visualization of peroxisomes by fluorescence microscopy, the peroxisomal targeting signal 1, PTS1, Ser-Lys-Leu, SKL, is fused to the extreme C-terminus of green fluorescent protein and DsRed, construction of plasmid pGBRH2-GFP-SKL, expression under the control of the strong Penicillium chrysogenum pcbC promoter, or by the lower-level, constitutive Aspergillus nidulans gpdA promoter in strain DS54465, an DELTAhdfA derivative of DS17690, transformation of protoplasts, overview
-
gene paaK, DNA and amino acid sequence determination, expression of His6-tagged enzyme in Escherichia coli
gene paaK1 is encoded in the paaFZJGIK1 operon located on the chromosome 1; gene paaK2 is encoded in the paaHK2paaG operon located on the chromosome 2
-
gene paaK1, paaK1 is a single copy gene, recombinant expression of His-tagged isozyme PaaK1 in Escherichia coli strain BL21Star(DE3), expression of selenomethionine-labeled PaaK1 in Escherichia coli strain 834(DE3); gene paaK2, recombinant expression of His-tagged isozyme PaaK2 in Escherichia coli strain BL21Star(DE3)
-
gene phl, sequence analysis, functional expression as C-terminally His6-tagged maltose binding protein fusion in Escherichia coli, expression of His-tagged mutants
gene phlC, cloning from DNA library in lambda ZAP II, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His8-tagged enzyme in Escherichia coli strain BL21 (DE3)-RP, subcloning in Escherichia coli strain DH5alpha, real-time quantitative RT-PCR expression analysis
genes paaF, DNA and amino acid sequence determination, strain Y2 is unique in having three paaF genes located within two complete copies of the paa gene clusters. Expression of both paaF and paaF3 is controlled by the PaaX repressor, expression analysis, overview, gene paaF2, adjacent to the StyS/StyR regulatory genes, belongs to the StyR regulon and is not subject to repression by PaaX, and the PpaaF2 promoter region contains a putative StyR binding site
-
overexpression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3-hydroxyphenylacetic acid induces the phenylacetic acid degradation pathway; 3-hydroxyphenylacetic acid induces the phenylacetic acid degradation pathway, while 4-hydroxyphenylacetic acid does not
Dnm1 and oleate suppress PCL and penicillin production
the enzyme is induced by phenylacetate
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F307A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
F335A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
V270A
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
V370A
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
Y267A
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
determination of of microbody-borne enzymes by analysis of putative microbody targeting singals and a proteomics based inventory of Penicillium chrysogenum microbody matrix proteins using nano-LC-MS/MS analysis
synthesis
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