Information on EC 1.3.1.32 - maleylacetate reductase

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

EC NUMBER
COMMENTARY hide
1.3.1.32
-
RECOMMENDED NAME
GeneOntology No.
maleylacetate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-oxoadipate + NAD(P)+ = 2-maleylacetate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,4-dichlorobenzene degradation
-
-
2,4,5-trichlorophenoxyacetate degradation
-
-
2,4,6-trichlorophenol degradation
-
-
3,4,6-trichlorocatechol degradation
-
-
3,5-dichlorocatechol degradation
-
-
3-chlorocatechol degradation I (ortho)
-
-
3-chlorocatechol degradation II (ortho)
-
-
4,5-dichlorocatechol degradation
-
-
4-aminophenol degradation
-
-
4-chlorocatechol degradation
-
-
4-hydroxyacetophenone degradation
-
-
4-nitrophenol degradation I
-
-
4-nitrophenol degradation II
-
-
4-sulfocatechol degradation
-
-
Benzoate degradation
-
-
Chlorocyclohexane and chlorobenzene degradation
-
-
chlorosalicylate degradation
-
-
Fluorobenzoate degradation
-
-
gamma-hexachlorocyclohexane degradation
-
-
gamma-resorcylate degradation I
-
-
gamma-resorcylate degradation II
-
-
Metabolic pathways
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Microbial metabolism in diverse environments
-
-
pentachlorophenol degradation
-
-
resorcinol degradation
-
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Toluene degradation
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3-chlorocatechol degradation
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resorcinol degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
3-oxoadipate:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
69669-65-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain R3
-
-
Manually annotated by BRENDA team
strain R3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain FLB 300, alpha-2 subclass of Proteobacteria in a new genus of the Agrobacterium-Rhizobium branch, designation by API 20 NE as Agrobacterium radiobacter
-
-
Manually annotated by BRENDA team
Bacteria FLB 300
strain FLB 300, alpha-2 subclass of Proteobacteria in a new genus of the Agrobacterium-Rhizobium branch, designation by API 20 NE as Agrobacterium radiobacter
-
-
Manually annotated by BRENDA team
chlorobenzene-degrading bacterium strain WR1306
chlorobenzene-degrading bacterium
-
-
Manually annotated by BRENDA team
strain AEO106
-
-
Manually annotated by BRENDA team
JMP 134-1
-
-
Manually annotated by BRENDA team
strain JMP134
-
-
Manually annotated by BRENDA team
strain JMP289
-
-
Manually annotated by BRENDA team
CA28
-
-
Manually annotated by BRENDA team
strain RW41
UniProt
Manually annotated by BRENDA team
strain ENV2030
-
-
Manually annotated by BRENDA team
strain ENV2030
-
-
Manually annotated by BRENDA team
strain AC866(pAC27)
-
-
Manually annotated by BRENDA team
strain WR1323
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain B1
-
-
Manually annotated by BRENDA team
strain JS100
-
-
Manually annotated by BRENDA team
strain JS6
-
-
Manually annotated by BRENDA team
strain PKO1
-
-
Manually annotated by BRENDA team
1CP; opacus 1CP, previously assigned R. erythropolis
-
-
Manually annotated by BRENDA team
strain ATCC 53874
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Sporotrichum pulverulentum
lignin-degrading white-rot fungus
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
cells bearing a disrupted hadD gene do not grow on plates with 2,4,6-TCP
physiological function
-
maleylacetate reductase is responsible for 2,4,6-trichlorophenol degradation in Ralstonia pickettii DTP0602
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3,5-trichloromaleylacetate + NADH
2,4-dichloro-3-oxohexanedioic acid + NAD+ + Cl-
show the reaction diagram
2,3-dibromomaleylacetate + NADH
3-bromo-4-oxohexanedioic acid + NAD+ + Br-
show the reaction diagram
2,3-dichloromaleylacetate + NADH
3-chloro-4-oxohexanedioic acid + NAD+ + Cl-
show the reaction diagram
2,4-dichlorophenoxyacetate + NADH
?
show the reaction diagram
2,5-dibromomaleylacetate + NADH
5-bromo-4-oxohex-2-enedioic acid + Br- + NAD+
show the reaction diagram
-
-
-
?
2,5-dichloromaleylacetate + NADH
2-chloro-3-oxohexanedioic acid + NAD+ + Cl-
show the reaction diagram
2-bromo-5-chloromaleylacetate + NADH
5-chloro-4-oxohex-2-enedioic acid + Br- + NAD+
show the reaction diagram
-
-
-
?
2-bromomaleylacetate + NADH
2-maleylacetate + NAD+ + Br-
show the reaction diagram
2-chloro-3-methylmaleylacetate + NADH
3-methyl-4-oxohex-2-enedioic acid + NAD+ + Cl-
show the reaction diagram
-
-
the product is further reduced to 3-methyl-4-oxohexanedioic acid under consumption of NADH
?
2-chloro-5-methylmaleylacetate + NADH
5-methyl-4-oxohex-2-enedioic acid + NAD+ + Cl-
show the reaction diagram
-
-
the product is further reduced to 2-methyl-3-oxohexanedioic acid under consumption of NADH
?
2-chloromaleylacetate + NAD(P)H
? + NAD(P)+
show the reaction diagram
2-chloromaleylacetate + NADH
2-maleylacetate + Cl- + NAD+
show the reaction diagram
2-chloromaleylacetate + NADH
maleylacetate + NAD+ + Cl-
show the reaction diagram
final enzyme in the pentachlorophenol biodegradation pathway which catalyzes the reductive dehalogenation of 2-chloromaleylacetate to maleylacetate and the subsequent reduction of malyelacetate to 3-oxoadipate
-
-
?
2-chloromaleylacetate + NADPH
2-maleylacetate + Cl- + NADP+
show the reaction diagram
2-fluoromaleylacetate + NADH
3-oxoadipate + NAD+ + F-
show the reaction diagram
-
-
-
?
2-maleylacetate + NAD(P)H
3-oxoadipate + NAD(P)+
show the reaction diagram
2-maleylacetate + NAD(P)H + H+
3-oxoadipate + NAD(P)+
show the reaction diagram
2-maleylacetate + NADH
3-oxoadipate + NAD+
show the reaction diagram
2-maleylacetate + NADPH
3-oxoadipate + NADP+
show the reaction diagram
2-methyl-3-chloromaleylacetate + NADH
3-chloro-2-methyl-4-oxohexanedioic acid + NAD+
show the reaction diagram
2-methylmaleylacetate + NAD(P)H
5-methyl-3-oxoadipate + NAD(P)+
show the reaction diagram
3-bromomaleylacetate + NADH
3-bromo-4-oxohexanedioic acid + NAD+
show the reaction diagram
3-chloromaleylacetate + NADH
3-chloro-4-oxohexanedioic acid + NAD+
show the reaction diagram
3-fluoromaleylacetate + NADH
2-fluoro-3-oxohexanedioic acid + NAD+
show the reaction diagram
-
-
-
?
3-methylmaleylacetate + NAD(P)H
4-methyl-3-oxoadipate + NAD(P)+
show the reaction diagram
5-bromomaleylacetate + NADH
2-bromo-3-oxohexanedioic acid + NAD+
show the reaction diagram
5-chloromaleylacetate + NADH
2-chloro-3-oxohexanedioic acid + NAD+
show the reaction diagram
5-fluoromaleylacetate + NADH
2-fluoro-3-oxohexanedioic acid + NAD+
show the reaction diagram
5-methylmaleylacetate + NAD(P)H
2-methyl-3-oxoadipate + NADP+
show the reaction diagram
cis,cis-3-hydroxymuconate + NADPH
? + NADP+
show the reaction diagram
maleylacetate + NADH
3-oxoadipate + NAD+
show the reaction diagram
-
-
-
?
phenoxyalacanoic herbicide 2,4,5-T + NADH
? + NAD+
show the reaction diagram
phenoxyalacanoic herbicide 2,4-D + NADH
? + NAD+
show the reaction diagram
trans,cis-3-hydroxymuconate + NADPH
? + NADP+
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
2,4-dichlorophenoxyacetate + NADH
?
show the reaction diagram
2-chloromaleylacetate + NADH
maleylacetate + NAD+ + Cl-
show the reaction diagram
Q8KN40
final enzyme in the pentachlorophenol biodegradation pathway which catalyzes the reductive dehalogenation of 2-chloromaleylacetate to maleylacetate and the subsequent reduction of malyelacetate to 3-oxoadipate
-
-
?
2-maleylacetate + NAD(P)H
3-oxoadipate + NAD(P)+
show the reaction diagram
2-maleylacetate + NAD(P)H + H+
3-oxoadipate + NAD(P)+
show the reaction diagram
2-maleylacetate + NADPH
3-oxoadipate + NADP+
show the reaction diagram
maleylacetate + NADH
3-oxoadipate + NAD+
show the reaction diagram
Q8KN40
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
129.02% activity compared to no addition 100%
Cd2+
39.52% activity compared to no addition 100%
Co2+
79.14% activity compared to no addition 100%
Cu2+
59.23% activity compared to no addition 100%
EDTA
112.93% activity compared to no addition 100%
Fe2+
118.90% activity compared to no addition 100%
Fe3+
134.89% activity compared to no addition 100%
K+
129% activity compared to no addition 100%
Mg2+
129.79% activity compared to no addition 100%
Mn2+
136.59% activity compared to no addition 100%
Na+
123.91% activity compared to no addition 100%
Ni2+
35.25% activity compared to no addition 100%
SDS
136.59% activity compared to no addition 100%
Zn2+
21.44% activity compared to no addition 100%
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-oxoadipate
-
competitive inhibition
CuSO4
maleylacetate
-
above 300 mM
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
total inhibition, reversed by thiol
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-Trichlorophenol
-
induction of MAR activity in wild type strain
2,4-dichlorophenoxyacetate
-
induction of MAR activity in wild type strain
histidine
-
histidine-HCl buffer results in considerably higher activity than corresponding bisTris-HCl or Tris-HCl buffers
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.347
2,3-dibromomaleylacetate
-
-
0.17 - 0.19
2,3-dichloromaleylacetate
0.279 - 0.288
2,5-dichloromaleylacetate
0.519
2-bromo-5-chloromaleylacetate
-
-
0.098 - 0.117
2-bromomaleylacetate
0.248
2-chloro-5-methylmaleylacetate
-
-
0.031 - 0.132
2-chloromaleylacetate
0.272 - 0.374
2-methylmaleylacetate
0.063 - 0.071
3-bromomaleylacetate
0.028 - 0.03
3-chloromaleylacetate
0.0043
3-fluoromaleylacetate
-
-
0.292 - 0.365
3-methylmaleylacetate
0.084 - 0.095
5-bromomaleylacetate
0.044 - 0.05
5-chloromaleylacetate
0.014 - 0.022
5-fluoromaleylacetate
0.11 - 0.133
5-methylmaleylacetate
0.025 - 0.09
maleylacetate
0.024 - 0.041
NADH
0.077 - 0.089
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 114
maleylacetate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
3-oxoadipate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00124
-
growth substrate L-tyrosine
0.0034
substrate 2-maleylacetate, crude enzyme extract
0.015
-
cells grown on phenol, 2-methylphenol or fructose
0.11
-
fructose grown cells
0.12
-
cells induced with phenoxyacetic acid
0.29
-
phenol grown cells
0.332
-
cell extracts of Pseudomonas putida KT2442 containing the pBS1hxqD plasmid
0.38
-
phenoxyacetic acid grown cells
0.4
-
strain WR1323
0.5
-
cells induced with 2,4-dichlorophenoxyacetic acid
0.65
-
resorcinol degradation in cell free extract
0.67
-
growth substrate succinate
0.68
-
strain R3
0.76
-
strain RHO1
0.8
-
strain B1
0.94
chlorobenzene-degrading bacterium strain WR1306
-
chlorobenzene-grown cells
1.112
-
cell extracts of Pseudomonas putida KT2442 containing the pBS1hqoD plasmid
5.983
-
cell extracts of Pseudomonas putida KT2442 containing the pBS1tcpD plasmid
27
above, purified enzyme
additional information
-
basal MAR activity under non-induced conditions in wild type
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 60
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-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Sporotrichum pulverulentum
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grown in presence of vanillate
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
-
strain PKO1
35000
-
2 * 35000, SDS-PAGE
36000
recombinant enzyme, determined by SDS-PAGE
36410
predicted
37100
-
SDS-PAGE
38000
-
SDS-PAGE
39183
x * 39183, mass spectrometry
56000
-
gel filtration, Superdex 200
72000
-
analytical gel filtration
81000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and SeMet-labeled PnpD, the sitting-drop vapour-diffusion method, 0.002 ml of 15 mg/ml protein in 20 mM Tris, pH 8.0, 5 mM NADH, and 20 mM NaCl are mixed with 0.002 ml of precipitant solution containing 0.2 M ammonium phosphate dibasic and 20% w/v PEG 3350, equilibration against 0.2 ml of reservoir solution, 20C, X-ray diffraction structure determination and analysis at 2.9 A resolution
sitting drop vapour diffusion method, using ammonium sulfate as the precipitating agent, at 20C
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
PcpE loses approximately 60% of its maximal activity
697528
5.8
-
activity drastically reduced at pH values below
390703
6.5 - 8.5
-
-
390700
8
PcpE loses approximately 60% of its maximal activity
697528
10
enzyme retains 58% activity after 30 min at pH 10
719179
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
enzyme retains 10% activity after 20 min at 60C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of DTT significantly stabilized enzyme
-
enzyme is very unstable
-
highly unstable and prone to precipitation at a concentration of 1 mg/ml or more in 50 mM Tris-Cl (pH 8.0) containing 50 mM NaCl at ambient temperatures. The stability of MaR can be improved by the addition of glycerol (at 30% v/v concentration) or by increasing the NaCl concentration (up to 1 M)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 100 mM Tris/HCl buffer, pH 7.0, containing 50% (vol/vol) glycerol, 1 mM dithioerythritol and 0.5 mM EDTA, purified enzyme retains 80% of its initial activity after storage for 2 months
-
-20C, 30% glycerol, 4 months, enzyme retains its activity
-23C, purified enzyme in 50 mM Tris-HCl, pH 7.5, 0.5 mM DTT, 0.1 mM EDTA after freezing, storage overnight and rethawing 35% loss of activity
-
-25C, 50 mM Tris/H2SO4 buffer, pH 7.6, can be stored for several months without loss of activity
-
-70C, 30% glycerol, 6 months, enzyme retains its activity
4C, 30% glycerol, 3 weeks, enzyme retains its activity
4C, purified enzyme can be stored in 50 mM Tris-HCl, pH 7.5, 0.5 mM DTT, 0.1 mM EDTA with slight loss of activity, 36% in 3 weeks
-
5C, 50 mM Tris/H2SO4 buffer, pH 7.6, can be stored for several days without loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by anion exchange chromatography
native enzyme, over 246fold by several chromatographic steps
purified 433fold using DEAR-Toyopearl column chromatography, phenyl-sepharose column chromatography and Mono Q column chromatography
-
purified from a MacA overexpressing Escherichia coli clone; purified from induced 4-chlorophenol grown cells
-
purified from recombinant Escherichia coli cells
-
recombinant His-tagged wild-type and SeMet-labeled PnpD from Escherichia coli BL21 (DE3) by nickel affinity chromatography
recombinant poly-His tagged PcpE is purified to higher than 95% purity using affinity chromatography with a Ni-NTA agarose column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli
-
cloning of the clcE gene encoding maleylacetate reductase from Pseudomonas sp. strain B13
-
expressed in Escherichia coli
gen tftE cloned and overexpressed in Escherichia coli
-
gene macA coding for one of two maleylacetate reductases cloned
-
gene macA, DNA sequence determination and analysis, gene cluster analysis, the cluster also comprises genes macB and macR, phylogenetic analysis, subcloning in Escherichia coli strain DH5alpha, overexpression in Escherichia coli strain BL21(DE3)
gene pnpD, expression of N-terminally His-tagged wild-type and SeMet-labeled PnpD in Escherichia coli BL21 (DE3)
into a pT7Blue T-Vector and expressed in Escherichia coli BL21 Star (DE3)
maleylacetate reductase gene cloned and sequenced
-
maleylacetate reductase genes from Alcaligenes eutrophus JMP289 and 335 cloned
-
overexpression in Escherichia coli BL21-AI cells
the chromosome of the nonfluorescent Pseudomonas sp. strain PKO1 cloned using plasmid pRO1727, the 0.5 kb BamH1 DNA fragment contains the gene for maleylacetate reductase, cloned mar gene is carried in cells of Pseudomonas aeruginosa and Pseudomonas putida
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the hqoD gene is cloned downstream of the arabinose-inducible promoter PBAD in the pBS1 vector to generate pBS1hqoD plasmids and transferred to Pseudomonas putida KT2442; the hxqD gene is cloned downstream of the arabinose-inducible promoter PBAD in the pBS1 vector to generate pBS1hxqD plasmids and transferred to Pseudomonas putida KT2442; the tcpD gene is cloned downstream of the arabinose-inducible promoter PBAD in the pBS1 vector to generate pBS1tcpD, plasmids and transferred to Pseudomonas putida KT2442
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
Sphingobium chlorophenolicum has assembled new catabolic pathways to degrade pentachlorophenol and use the ring-cleavage products as their carbon sources
additional information
Show AA Sequence (211 entries)
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