Information on EC 3.7.1.9 - 2-hydroxymuconate-6-semialdehyde hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.7.1.9
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxymuconate-6-semialdehyde hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxymuconate-6-semialdehyde + H2O = formate + 2-oxopent-4-enoate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-C bonds in ketonic substances
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
-
-
catechol degradation to 2-oxopent-4-enoate I
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
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Styrene degradation
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Xylene degradation
-
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phenol degradation
-
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxymuconate-6-semialdehyde formylhydrolase
The enzyme is involved in the degradation of catechols.
CAS REGISTRY NUMBER
COMMENTARY hide
54004-61-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Rue61a
-
-
Manually annotated by BRENDA team
Rue61a
-
-
Manually annotated by BRENDA team
strain 206
-
-
Manually annotated by BRENDA team
strain 206
-
-
Manually annotated by BRENDA team
ATCC 17707
-
-
Manually annotated by BRENDA team
JM83
-
-
Manually annotated by BRENDA team
JM83
-
-
Manually annotated by BRENDA team
ATCC27551
-
-
Manually annotated by BRENDA team
ATCC27551
-
-
Manually annotated by BRENDA team
AW-2
-
-
Manually annotated by BRENDA team
CF600
-
-
Manually annotated by BRENDA team
gene pheD encoded in the phe lower operon of the TOU catabolic pathway
UniProt
Manually annotated by BRENDA team
OX1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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
1H-3-hydroxy-4-oxoquinaldine + H2O
?
show the reaction diagram
2-hydroxy-5-methyl-6-oxohepta-2,4-dienoate + H2O
?
show the reaction diagram
-
no activity with isoenzyme HODHI, 41% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHII
-
-
?
2-hydroxy-5-methyl-muconic semialdehyde + H2O
?
show the reaction diagram
-
3% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI. 5% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
show the reaction diagram
2-hydroxy-5-methylmuconic semialdehyde + H2O
?
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
show the reaction diagram
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
show the reaction diagram
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
show the reaction diagram
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxy-6-oxoocta-2,4-dienoate + H2O
?
show the reaction diagram
2-hydroxy-7-methyl-6-oxoocta-2,4-dienoate + H2O
?
show the reaction diagram
-
149% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI, no activity with isoenzyme HODHII
-
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxymuconic semialdehyde + H2O
?
show the reaction diagram
3-allylcatechol ring-fission product + H2O
?
show the reaction diagram
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-allylcatechol
-
-
?
3-ethylcatechol ring-fission product + H2O
?
show the reaction diagram
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-ethylcatechol
-
-
?
3-methylcatechol ring-fission product + H2O
?
show the reaction diagram
3-propylcatechol ring-fission product + H2O
?
show the reaction diagram
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol
-
-
?
4-chlorocatechol ring-fission product + H2O
?
show the reaction diagram
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol
-
-
?
4-ethylcatechol ring-fission product + H2O
?
show the reaction diagram
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-ethylcatechol
-
-
?
4-methylcatechol ring-fission product + H2O
?
show the reaction diagram
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-methylcatechol
-
-
?
4-propylcatechol ring-fission product + H2O
?
show the reaction diagram
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-propylcatechol
-
-
?
catechol ring-fission product + H2O
?
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-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
show the reaction diagram
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
show the reaction diagram
G3KFX4
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Fe2+, Ca2+, Cu2+, Mg2+, Mn2+, Co2+, Li2+, and Zn2+ have no effect
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
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-
DEPC
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inhibits by 82%
diethyl dicarbonate
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diisopropyl fluorophosphate
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-
iodoacetamide
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-
Mn2+
-
isoenzyme HODHI is inhibited, isoenzyme HODHII is activated
phenylmethylsulfonyl fluoride
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-
Sodium arsenite
-
-
tosyl-Phe chloromethyl ketone
-
-
additional information
-
N-ethylmaleimide and p-chloromercuribenzoate show no significant effect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mn2+
-
isoenzyme HODHI is inhibited, isoenzyme HODHII is activated
additional information
-
EDTA has no effect
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027 - 0.044
1H-3-Hydroxy-4-oxoquinaldine
0.2315
2-hydroxy-5-methylmuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25C
-
0.0074
2-hydroxy-5-methylmuconic semialdehyde
-
-
0.00045 - 0.01
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
0.0008 - 0.022
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
0.0012 - 0.058
2-hydroxy-6-oxohepta-2,4-dienoate
0.0018 - 0.015
2-hydroxy-6-oxoocta-2,4-dienoate
0.232
2-hydroxymuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25C
0.0057 - 62
2-hydroxymuconic semialdehyde
0.0075 - 0.023
3-methylcatechol ring-fission product
-
0.085 - 0.35
catechol ring-fission product
-
0.037
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-allylcatechol
-
-
-
0.015
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-ethylcatechol
-
-
-
0.036
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol
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-
0.005
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol
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-
-
0.122
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol
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-
0.022
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-ethylcatechol
-
-
-
0.01
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-methylcatechol
-
-
-
0.023
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-propylcatechol
-
-
-
0.03
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol
-
-
-
additional information
additional information
steady-state kinetic analysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.15
2-hydroxy-5-methylmuconate-6-semialdehyde
Pseudomonas sp.
G3KFX4
recombinant enzyme, pH 7.5, 25C
-
16
2-hydroxy-5-methylmuconic semialdehyde
Flavobacterium sp.
-
-
0.002 - 0.037
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
0.41 - 29
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
0.3 - 81
2-hydroxy-6-oxohepta-2,4-dienoate
1.3 - 78
2-hydroxy-6-oxoocta-2,4-dienoate
18.2
2-hydroxymuconate-6-semialdehyde
Pseudomonas sp.
G3KFX4
recombinant enzyme, pH 7.5, 25C
42
2-hydroxymuconic semialdehyde
Flavobacterium sp.
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-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50
2-hydroxy-5-methylmuconate-6-semialdehyde
Pseudomonas sp.
G3KFX4
recombinant enzyme, pH 7.5, 25C
206962
2200
2-hydroxy-6-oxohepta-2,4-dienoate
Pseudomonas sp.
G3KFX4
recombinant enzyme, pH 7.5, 25C
2635
780
2-hydroxymuconate-6-semialdehyde
Pseudomonas sp.
G3KFX4
recombinant enzyme, pH 7.5, 25C
5232
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.18
purified recombinant enzyme, substrate 2-hydroxy-5-methylmuconate-6-semialdehyde, pH 7.5, 25C
3.87
purified recombinant enzyme, substrate 2-hydroxymuconate-6-semialdehyde, pH 7.5, 25C
6.1
-
S103A mutant
10.1
-
isoenzyme HODHII
12.1
-
mutant S101A
17.4
-
isoenzyme HODHI
17.6
-
mutant D233A
28.1
-
His-tagged HOD
28.4
purified recombinant enzyme, substrate 2-hydroxy-6-oxohepta-2,4-dienoate, pH 7.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
pH 7.6: 75-80% of the activity at pH 8.6, pH 9.0: marked decrease in activity above pH 9.0, similar pH profile of both isoenzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
-
loses just 20% activity after incubation for 2 hours
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 85
-
above 75C enzyme activity declines rapidly
5 - 60
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full enzyme activity up to 20C for 30 min, and ca. 80% between 30 and 50C, almost completely inactivated above 60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.93
sequence calculation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30600
-
N-terminal sequence analysis
30965
-
x * 30965, calculation from nucleotide sequence
31489
-
2 * 32000, SDS-PAGE, 2 * 31489, amino acid sequence
31840
-
sequence analysis
32000
-
2 * 32000, SDS-PAGE, 2 * 31489, amino acid sequence
34400
-
3 * 34400, isoenzyme HODHI, SDS-PAGE of 2-mercaptoethanol reduced enzyme
36700
-
3 * 36700, isoenzyme HODHII, Alcaligenes eutrophus, SDS-PAGE of 2-mercaptoethanol reduced enzyme
58000
-
gel filtration
65000
-
gel filtration
104000
-
sedimentation equilibrium analysis
116000
-
isozyme HODHII, sedimentation equilibrium analysis
120000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
trimer
-
3 * 34400, isoenzyme HODHI, SDS-PAGE of 2-mercaptoethanol reduced enzyme; 3 * 36700, isoenzyme HODHII, Alcaligenes eutrophus, SDS-PAGE of 2-mercaptoethanol reduced enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
A129V mutant, at 1.65 A resolution, crystals of the A129V mutant isomorphous with the S103A crystals
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
-
674958
7 - 8
-
optimal stability at pH 7-8, rapid loss of activity below pH 5 and above pH 9.5
247052
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
stable for 3 days
42
-
wild-type enzyme loses 50% of its activity after 15 min, mutant enzyme H36A loses 50% of its initial activity after 1.6 min, mutant enzyme F108M loses 60% of its initial activity after 60 min, mutant enzyme S152A loses 50% of its initial activity after 2.2 min, mutant enzyme H249A loses 50% of its initial activity after 1.1 min
45
-
isoenzyme HODHII is inactivated after 2 min, isoenzyme HODHI is inactivated after 4 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20% glycerol, 15 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATCC 17707, strain 345, isozyme HODHII: TOL-like plasmid encoded enzyme, strain RA1012, isozyme HODHI: chromosomally-encoded enzyme
-
by affinity chromatography
-
His-tagged HOD purified by Ni2+/NTA affinity chromatography
-
recombinant enzyme from Escherichia coli strain JM109 by anion exchange chromatography and gel filtration
to homogeneity, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli XL1-Blue M15
-
gene pheD encoded in the phe lower operon of the TOU catabolic pathway, DNA and amino acid sequence determination and analysis, genetic organization, recombinant expression in Escherichia coli strain JM109
into pUC119 and overexpression in Escherichia coli
-
overexpression as an N-terminal His-tag from pSM12 in Escherichia coli BL21(DE3), or from plasmid pSM13 in Pseudomonas aeruginosa PAO1161
-
subcloned in Escherichia coli IPTG inducible vectors
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D233A
-
residual activity of 62.6%
S101A
-
residual activity of 43.1%
D233A
-
residual activity of 62.6%
-
S101A
-
residual activity of 43.1%
-
A129V
-
improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
A129V/I199V/V227I
-
combination of mutations incompatible for correct folding
D224A
-
aggregates into inclusion bodies and thus can not be purified
F104M
-
mutation does not have any significant effect on enzyme characteristics
H252A
-
aggregates into inclusion bodies and thus can not be purified
I199V
-
improved catalytic efficiency than the wild type enzyme
I199V/V2271
-
combination of mutations incompatible for correct folding
S103A
-
has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
S34A
-
lower Km and turnover rates compared to wild-type
S34G
-
lower Km and turnover rates compared to wild-type
V227I
-
improved catalytic efficiency than the wild type enzyme
A129V
-
improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
-
A129V/I199V/V227I
-
combination of mutations incompatible for correct folding
-
I199V
-
improved catalytic efficiency than the wild type enzyme
-
I199V/V2271
-
combination of mutations incompatible for correct folding
-
V227I
-
improved catalytic efficiency than the wild type enzyme
-
D224A
-
aggregates into inclusion bodies and thus can not be purified
-
H252A
-
aggregates into inclusion bodies and thus can not be purified
-
S103A
-
has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
-
C254S
-
1% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes
D228A
-
activity below detection
D65V
-
activity below detection. Unstable, decreases in cellular extrects after 10 min
F108M
-
18% of the activity of wild-type enzyme, enzyme displays greater thermostability than the wild-type enzyme
H249A
-
26% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes, severe decrease in protein stability compared to wild-type enzyme
H256A
-
activity below detection
H36A
-
15% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
S107A
-
activity below detection
S107C
-
0.44% of the activity of wild-type enzyme
S152A
-
80% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
Show AA Sequence (142 entries)
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