Information on EC 1.13.11.3 - protocatechuate 3,4-dioxygenase

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

EC NUMBER
COMMENTARY hide
1.13.11.3
-
RECOMMENDED NAME
GeneOntology No.
protocatechuate 3,4-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-hydroxymandelate degradation
-
-
Benzoate degradation
-
-
gallate degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Polycyclic aromatic hydrocarbon degradation
-
-
protocatechuate degradation II (ortho-cleavage pathway)
-
-
SYSTEMATIC NAME
IUBMB Comments
protocatechuate:oxygen 3,4-oxidoreductase (decyclizing)
Requires Fe3+. The enzyme, which participates in the degradation of aromatic compounds, catalyses the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring. The type of cleavage leads to mineralization via the intermediate 3-oxoadipate.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-47-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ADP1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 80-1, derivative of ATCC 14987
-
-
Manually annotated by BRENDA team
strain 80-1, derivative of ATCC 14987
-
-
Manually annotated by BRENDA team
strain K24, enzyme is induced by growth on p-hydroxybenzoate
-
-
Manually annotated by BRENDA team
strain K24, enzyme is induced by growth on p-hydroxybenzoate
-
-
Manually annotated by BRENDA team
strain S2, protocatechuate 3,4-dioxygenase I and II
-
-
Manually annotated by BRENDA team
formerly classified as Pseudomonas cepacia
-
-
Manually annotated by BRENDA team
Geobacillus sp.
strain S1, protocatechuate 3,4-dioxygenase II
-
-
Manually annotated by BRENDA team
Leifsonia sp.
-
-
-
Manually annotated by BRENDA team
enzyme is induced in cells grown on protocatechuic acid or analogues
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas fluorescens
-
-
-
Manually annotated by BRENDA team
Nocardia erythropolis
-
-
-
Manually annotated by BRENDA team
wood-degrading fungus
-
-
Manually annotated by BRENDA team
strain B-10, enzyme is induced in cells grown on 4-hydroxybenzoate
-
-
Manually annotated by BRENDA team
strain A.3.12.
-
-
Manually annotated by BRENDA team
strain A.3.12.
-
-
Manually annotated by BRENDA team
Pseudomonas mendocina P2d, an array of colors are formed when Pseudomonas mendocia P2d cells grow in sodium or tyrosine, which is ascribed to the presence of multiple enzyms: catechol-1,2-doxygenase, catechol-2,3-dioxygenase, protocatechuate-3,4-dioxygenase, and tyrosinase
-
-
Manually annotated by BRENDA team
Roseobacter sp.
isolates GAI-16, S25com04 and IC4, enzyme activity is induced by growth on p-hydroxybenzoate
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
enzyme activity is induced by growth on p-hydroxybenzoate
-
-
Manually annotated by BRENDA team
Sulfitobacter sp.
strain EE-36, Y3F, and Y4I
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
show the reaction diagram
3,4-dihydroxybenzoate + O2
?
show the reaction diagram
3,4-dihydroxybenzoate + O2
beta-carboxy-cis,cis-muconate
show the reaction diagram
-
-
-
-
?
3,4-dihydroxymandelic acid + O2
?
show the reaction diagram
3,4-dihydroxyphenylacetate + O2
?
show the reaction diagram
3,4-dihydroxyphenylalanine + O2
?
show the reaction diagram
Nocardia erythropolis
-
at 10.7% the rate of protocatechuic acid oxidation
-
-
?
3,4-dihydroxyphenylpropionic acid + O2
?
show the reaction diagram
-
-
-
-
-
3-(3,4-dihydroxyphenyl)propionate + O2
?
show the reaction diagram
-
protocatechuate 3,4-dioxygenase II
-
-
?
3-methylcatechol + O2
2-methylmuconate
show the reaction diagram
4-cresol + O2
?
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
show the reaction diagram
4-methylcatechol + O2
?
show the reaction diagram
-
-
-
-
?
4-sulfocatechol + O2
3-sulfomuconate
show the reaction diagram
5-fluoro-protocatechuic acid + O2
5-fluoro-3-carboxy-cis,cis-muconate
show the reaction diagram
-
at 2.1% the rate of protocatechuic acid oxidation
-
?
6-chloro-protocatechuate + O2
6-chloro-3-carboxy-cis,cis-muconate
show the reaction diagram
-
at 4.3% the rate of protocatechuic acid oxidation
-
?
caffeic acid + O2
?
show the reaction diagram
catechin + O2
?
show the reaction diagram
-
-
-
-
?
catechol + O2
cis,cis-muconate
show the reaction diagram
catechol + O2
muconate
show the reaction diagram
gallate + O2
?
show the reaction diagram
-
-
-
-
?
L-DOPA + O2
?
show the reaction diagram
-
-
-
-
?
protocatechuate + O2
3-carboxy-cis,cis-muconate
show the reaction diagram
protocatechuate + O2
beta-carboxy-cis-cis-muconate
show the reaction diagram
protocatechuic acid + O2
3-carboxy-cis,cis-muconic acid
show the reaction diagram
Geobacillus sp.
-
-
-
-
?
pyrogallol + O2
?
show the reaction diagram
trans-3,4-dihydroxycinnamate + O2
?
show the reaction diagram
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
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
show the reaction diagram
protocatechuate + O2
beta-carboxy-cis-cis-muconate
show the reaction diagram
protocatechuic acid + O2
3-carboxy-cis,cis-muconic acid
show the reaction diagram
Geobacillus sp.
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
Leifsonia sp.
-
increases enzyme activity for both cell-free and immobilized extracts by 8% and 44%, respectively
Fe2+
-
activates by 29% at 3 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
0.005 mM, approx. 50% inhibition after 30 min, complete inhibition after 60 min, complete restoration of inactivated enzyme by addition of excess ferric EDTA complex
2,3-Dihydroxybenzoate
2,4-dihydroxybenzoic acid
-
competitive inhibition
2,5-Dihydroxybenzoate
-
-
2-Fluoro-4-hydroxybenzoate
-
-
2-Hydroxyisonicotinic acid N-oxide
2-Hydroxypyridine N-oxide
-
-
3,4-Dihydroxyacetophenone
3,4-dihydroxybenzoate
-
-
3,4-dihydroxycinnamic acid
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-dihydroxyphenylacetic acid
3,4-Dihydroxyphenylpropionate
-
-
3,5-Dichloro-4-hydroxybenzoate
-
-
3-Bromo-4-hydroxybenzoate
-
-
3-Chloro-4-hydroxybenzoate
-
-
3-Fluoro-4-hydroxybenzoate
3-hydroxybenzoate
3-hydroxyphenylacetic acid
-
-
3-Nitrophenol
-
0.006 mM, 56% inhibition
4-(dimethylamino)benzaldehyde
-
-
4-Fluoro-3-hydroxybenzoate
4-hydroxybenzoate
4-hydroxymercuribenzoate
4-hydroxyphenylacetic acid
-
-
4-Methylcatechol
4-nitrocatechol
4-sulfocatechol
alpha-chloro-3,4-dihydroxyacetophenone
-
-
Ca2+
Nocardia erythropolis
-
-
caffeic acid
-
-
catechol
Cd2+
-
inhibits 40% at 3 mM
Co2+
-
inhibits 48.5% at 3 mM
Cu2+
-
inhibits 70% at 3 mM
Fe3+
-
inhibits 77% at 3 mM
Ferrous ammonium sulfate
-
-
Hg2+
Nocardia erythropolis
-
0.1 mM, 45% inhibition
iodoacetate
isonicotinic acid N-oxide
-
-
Isovanillate
-
-
KF
-
50 mM, 34% inhibition
Mn2+
-
inhibits 19% at 3 mM
N-ethylmaleimide
Na2HAsO4
Nocardia erythropolis
-
0.1 mM, 50% inhibition
Nickel ammonium sulfate
-
-
o-Chloranil
-
0.006 mM, 51% inhibition
p-chloromercuribenzoate
-
0.05 mM, 47% inhibition
Pb2+
Nocardia erythropolis
-
-
Protocatechualdehyde
protocatechuate
Protocatechuic acid methyl ester
-
-
vanillate
-
-
Zn2+
-
inhibits 49% at 3 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Na2SO4
-
nonessential activator
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029 - 0.142
3,4-dihydroxybenzoate
0.014
4-Cresol
0.042 - 0.058
4-sulfocatechol
0.014
caffeic acid
0.033
catechol
Geobacillus sp.
-
-
0.04
FeSO4
-
-
0.002
gallate
-
pH 7.5, 38C
0.014
L-Dopa
-
pH 7.5, 38C
0.006 - 0.8
O2
0.002 - 0.33
protocatechuate
0.014
pyrogallol
-
pH 7.5, 38C
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 758
3,4-dihydroxybenzoate
14.6
4-sulfocatechol
Agrobacterium tumefaciens
-
protocatechuate 3,4-dioxgenase type II
0.007 - 120
O2
0.01 - 100
protocatechuate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
2,5-Dihydroxybenzoate
-
-
0.01
2-Fluoro-4-hydroxybenzoate
-
-
0.0068
2-Hydroxyisonicotinic acid N-oxide
-
apparent Ki, irreversible binding
3.9
2-Hydroxypyridine N-oxide
-
apparent Ki, inhibition is not freely reversible
0.13
3,4-Dihydroxyacetophenone
-
-
0.013
3,4-Dihydroxyphenylacetate
-
-
0.041
3,4-dihydroxyphenylacetic acid
-
-
0.018
3,4-Dihydroxyphenylpropionate
-
-
0.044
3,5-Dichloro-4-hydroxybenzoate
-
-
0.018
3-Bromo-4-hydroxybenzoate
-
-
0.0032
3-Chloro-4-hydroxybenzoate
-
-
0.0003 - 0.01
3-Fluoro-4-hydroxybenzoate
0.004
3-hydroxybenzoate
-
-
0.3 - 0.8
4-Fluoro-3-hydroxybenzoate
0.087 - 0.24
4-hydroxybenzoate
0.44
4-Methylcatechol
-
-
0.0006 - 0.0048
4-nitrocatechol
0.032 - 0.053
4-sulfocatechol
0.17
alpha-chloro-3,4-dihydroxyacetophenone
-
-
0.38 - 0.7
catechol
1.3
isonicotinic acid N-oxide
-
-
0.02
Isovanillate
-
-
0.001 - 0.073
Protocatechualdehyde
0.066 - 0.102
protocatechuate
0.4
protocatechuic acid methylester
-
-
0.003
vanillate
-
-
additional information
additional information
-
rates (s-1) and dissociation constants (microM) for 4-hysroxybenzoate: wild type: k+2 = 42, k-2 = 14, k+2 + k-2 = 56, K1 = 700, Kd = 170, Y408H: k+2 + k-2 = 2.3, Y408C: k+2 + k-2 = 0.7, Y408F: k+2 + k-2 = 0.9; substrate dissociation constant for 3-hydroxybenzoate: wild type = 3500 microM, Y408H = 180 microM, Y408E = 210 microM, Y408C = 2500 microM, Y408F = 1800 microM; substrate dissociation constant for 4-hydroxybenzoate: wild type = 300 microM, Y408H = 6.3 microM, Y408C = 51 microM, Y408F = 12 microM
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0081
-
-
0.113
-
activity in E. coli cell extracts expressing the recombinant enzyme
0.31
Roseobacter sp.
-
Rosebacter isolate GAI-16, enzyme activity in cell extracts
0.34
-
soluble enzyme
0.39
-
enzyme immobilized on glass-beads
0.46
-
enzyme activity in cell extracts
0.73
Roseobacter sp.
-
Rosebacter isolate S25com04, enzyme activity in cell extracts
0.88
Roseobacter sp.
-
Rosebacter isolate IC4, enzyme activity in cell extracts
2.98
-
inductor 3,4-dihydroxybenzoic acid, cell-free extract from Stenotrophomonas maltophilia
5.2
-
type II protocatechuate 3,4-dioxygenase, oxidation of 4-sulfocatechol
6.37
-
inductor 4-hydroxybenzoic acid, cell-free extract from Stenotrophomonas maltophilia
8.7
-
inductor vanillic acid, cell-free extract from Stenotrophomonas maltophilia
16.7
-
type II protocatechuate 3,4-dioxygenase, oxidation of 4-sulfocatechol
34.2
Geobacillus sp.
-
-
37.2
-
recombinant enzyme
105
-
type I protocatechuate 3,4-dioxygenase
121.7
-
purified native enzyme, pH 7.5, 38C
350
Geobacillus sp.
-
activity at the 10th h of the exponential growth phase
additional information
Nocardia erythropolis
-
379 mg O2/min/ml
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
-
completely inactive above pH 6.5
7.3 - 8.5
-
immobilized enzyme
8.3 - 8.4
-
free enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
Leifsonia sp.
-
activity range, profile overview
6 - 9
Geobacillus sp.
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 65% of maximal activity
6.5 - 8
Leifsonia sp.
-
80% of maximal activity within this range
additional information
-
activity increases steadily up to pH 9.0, above pH 9.0 the enzyme begins to undergo spontaneous oxidation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
free enzyme, 9% activity at 60C, no activity at 80C
45
-
immobilized enzyme
55
Leifsonia sp.
-
optimum for the immobilized enzyme extract
60
Geobacillus sp.
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 80
-
immobilized enzyme: 78% activity at 60C, 75% activity at 80C
50 - 70
Geobacillus sp.
-
50C: about 55% of maximal activity, 70C: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
localized in 100000 g supernatant, completely absent in mitochondrial, microsomal and chloroplast fraction
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
189900
-
gel filtration
190000
-
gel filtration
202000
-
meniscus depletion
204000
-
sedimentation equilibrium
220000
-
gel filtration
315000
-
analytical ultracentrifugation
480000
510000
-
gel filtration
590000
-
ultracentrifugation
677000
-
sedimentation velocity analysis
700000
-
diffusion data
783100
-
calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
hexamer
octamer
tetramer
-
alpha,beta, 2 * 22280 + 2 * 26630, holoenzyme probably contains 6 alpha2,beta2 tetramers, amino acid sequence
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
carbohydrate contributes less than 0.2% to the mass of the holoenzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, hanging drop method with 1.8 M ammonium sulfate, 50 mM Tris-HCl pH 7.0 in the reservoir and 10 mg/ml enzyme in the drop at 18C, crystals grow as perfect dodecahedrons, crystal structure with 2.2 A resolution
-
microdialysis of approx. 0.05 ml of enzyme solution, 80 mg/ml against 10 ml volumes of buffered solutions, large single crystals
-
vapor equilibration at room temperature from solutions containing potassium phosphate pH 7.5, 1.08-1.2 M reservoir concentrations, initial enzyme concentration 6.7-10.5 mg/ml
-
addition of 0.1 ml 1 M 2-mercaptoethanol to 10 ml enzyme solution in 50 mM Tris buffer pH 8.5, rhombic crystals appear after 1 week in a refrigerator, crystallization is also achieved by adding 1 mM iodoacetamide instead of mercaptoethanol or by dialyzing the enzyme against cold, destilled water for 2 days
-
X-ray crystallography
-
free interface diffusion cell, equal volumes of concentrated enzyme and ammonium sulfate solutions ranging from 37-47% saturation, 4C, 2.5 A resolution
-
vapor diffusion in hanging drops, crystal structure at 2.1-2.2 A resolution
-
vapor diffusion with ammonium sulfate as the precipitant at 4C, recombinant wild-type and Y447H mutant enzyme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.6
-
24C, 1 week, less than 10% loss of activity
439483
7.6 - 8.6
Nocardia erythropolis
-
most stable
439502
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
stable for long periods
20 - 50
-
purified enzyme, 50 min, pH 7.5, relatively stable
42
Nocardia erythropolis
-
1 h, stable below
65
-
soluble and immobilized enzyme, 15 min, complete loss of activity
70
-
purified enzyme, 20 min, pH 7.5, loss of 95% activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme immobilized on porous glass beads is stable over wide ranges of pH and temperature
-
immobilization: slight increase of thermal stability, soluble and immobilized enzyme exhibit substantial activity in 2 M urea
-
inactivated by reducing agents
-
lyophilization, stable
-
no loss of activity over a period of 78 d under aerobic conditions at 15C at pH 7.0, pH 8.0 or pH 9.0
-
UV irradiation: 38000 ergs per m2, inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for several years
-
0-3C, several weeks, no loss in activity
-
4C, pH 8.5, 6 months
-
5C, long periods, no loss in activity
-
stable only 7 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-cellulose
-
ammonium sulfate, DEAE-cellulose, Bio-gel agarose, DEAE-cellulose
-
ammonium sulfate, DEAE-cellulose, Sephadex G-200
-
ammonium sulfate, DEAE-Sepharose, octyl-Sepharose, Phenyl-sepharose, recombinant enzyme
-
ammonium sulfate, DEAE-Sepharose, Phenyl-Sepharose
-
ammonium sulfate, Q-Sepharose, partial purification
-
ammonium sulfate, Sephacryl S 300, DEAE-Sephadex A50
-
cells harvested by centrifugation, washed twice with 50 mM sodium phosphate buffer, pH 7.0 containing 10% glycerol, disruption with solicitor, centrifuged, supernatant stored at -20C
Geobacillus sp.
-
enzymes from Escherichia coli: DEAE-Sepharose Fast Flow column (5.5 x 19 cm), Phenyl-Sepharose CL-4B column (4.5 x 22.5 cm), Sephacryl S-300 column (3 x 97.5 cm); enzymes from Pseudomonas florescens
-
native enzyme 296.8fold by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography
-
Q-Sepharose FF, ammonium sulfate, Sephacryl S-300HR, phenyl-superose HR5/5, Mono Q, type II protocatechuate 3,4-dioxygenase; Q-Sepharose FF, ammonium sulfate, Sephacryl S-300HR, Phenyl-Superose, type I protocatechuate 3,4-dioxygenase
-
Q-Sepharose FF, ammonium sulfate, Superdex 200, Fractogel, type II protocatechuate 3,4-dioxygenase
-
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli, the genetic locus ncg12314-ncg12315 of the Corynebacterium glutamicum encodes a putative protocatechuate 3,4-dioxygenase
-
expression in Escherichia coli
-
expression of protocatechuate 3,4-dioxygenase II in Escherichia coli
-
expression of wild-type and Y447H mutant enzyme in Pseudomonas fluorescens
-
expression of wild-type, W153V, R142K and R142/W153V double mutant of protocatechuate 3,4-dioxygenase I in Escherichia coli
-
phylogenetic tree
Leifsonia sp.
-
the enzyme containing the Y408E mutation is expressed in Pseudomonas fluorescens; the enzymes containing the Y408C, Y408F and Y408H mutation are expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Crc induces carbon catabolite repression of protocatechuate 3,4-dioxygenase. Crc is not involved in carbon catabolite repression of the protocatechuate 3,4-dioxygenase operon (pca-qui) at the transcriptional level. Addition of acetate and succinate to medium containing a carbon source leads to repression of protocatechuate 3,4-dioxygenase by 95%, whereas other organic acids, like pyruvate, do not have a repressing effect
protocatechuate induces PcaHG activity and PcaO regulates the key step in aromatic cleavage during PCA degradation at the pcaHG transcriptional level
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA319-322
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turnover-number is 4.14fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.1fold lower than that of the wild-type enzyme
R457S
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turnover-number is 1333fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.2fold lower than that of the wild-type enzyme
R142K
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like wild-type no acticity of mutated protocatechuate 3,4-dioxygenase I with 4-sulfocatechol
R142K/W153V
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protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol
R153V
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protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol
Y408F
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iron is not tightly bound, the Y408F mutant does not reconstitute above half-occupancy and loses color during crystallization attempts. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly.
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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use in flushing and scrubbing oxygen out of instruments such as stopped-flow spectrophotometers
degradation
environmental protection
Geobacillus sp.
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the purified enzyme can be used in bioremediation of polluted groundwater or soil contaminated with various aromatic compounds ranging from monocyclic to polycyclic
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