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Information on EC 3.7.1.9 - 2-hydroxymuconate-6-semialdehyde hydrolase
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3.7.1.9 2-hydroxymuconate-6-semialdehyde hydrolaseIUBMB Comments
The enzyme is involved in the degradation of catechols.
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Word Map
- 3.7.1.9
- catechols
-
extradiol
- sphingomonas
- 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
- 2-hydroxy-6-oxohepta-2,4-dienoate
-
lignin-related
- 4-hydroxy-2-oxovalerate
-
xylf
- paucimobilis
- 5-carboxyvanillate
- 4-oxalocrotonate
- m-cresol
-
isopropylbenzene
- toluate
- 3-methylcatechol
- molecular biology
The enzyme appears in viruses and cellular organisms
Synonyms
2-hydroxymuconic semialdehyde hydrolase, meta-cleavage compound hydrolase, hydroxymuconic semialdehyde hydrolase, 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate, 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase, 2-hydroxymuconate semialdehyde hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase
2-hydroxy-6-oxohepta-2,4-dienoate hydrolase
-
-
-
-
2-hydroxymuconate semialdehyde hydrolase
2-hydroxymuconate-semialdehyde hydrolase
-
-
-
-
2-hydroxymuconic semialdehyde hydrolase
6-isopropyl-HODA hydrolase
CumD
HcdC
HMSH
HOD
HOD hydrolase
-
-
-
-
hydrolase, 2-hydroxymuconate semialdehyde
-
-
-
-
hydroxymuconic semialdehyde hydrolase
meta-cleavage compound hydrolase
meta-cleavage product hydrolase
MfhA
XylF
-
-
-
-
2-hydroxymuconate semialdehyde hydrolase
-
-
-
-
2-hydroxymuconic semialdehyde hydrolase
-
-
-
-
HMSH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-hydroxymuconate-6-semialdehyde + H2O = formate + 2-oxopent-4-enoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-C bonds in ketonic substances
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxymuconate-6-semialdehyde formylhydrolase
The enzyme is involved in the degradation of catechols.
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CAS REGISTRY NUMBER
COMMENTARY
54004-61-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxy-5-methyl-6-oxohepta-2,4-dienoate + H2O
?
-
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
?
-
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-7-methyl-6-oxoocta-2,4-dienoate + H2O
?
-
149% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI, no activity with isoenzyme HODHII
-
-
?
3-allylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-allylcatechol
-
-
?
3-ethylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-ethylcatechol
-
-
?
3-propylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol
-
-
?
4-chlorocatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol
-
-
?
4-ethylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-ethylcatechol
-
-
?
4-methylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-methylcatechol
-
-
?
4-propylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-propylcatechol
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-allylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-ethylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-ethylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-methylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-propylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol + H2O
?
-
-
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
prepared from 4-methylcatechol
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
prepared from 4-methylcatechol
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
slight hydrolysis
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
slight hydrolytic activity
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
slight hydrolytic activity
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
slight hydrolysis
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
prepared from 3-methylcatechol, best substrate
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
prepared from 3-methylcatechol, best substrate
-
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
metabolism of 2-hydroxymuconate 6-semialdehyde through HMS hydrolase is predominant compared to metabolism by HMS dehydrogenase
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
metabolism of 2-hydroxymuconate 6-semialdehyde through HMS hydrolase is predominant compared to metabolism by HMS dehydrogenase
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
31% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI. 12% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHII
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
2-hydroxymuconate semialdehyde
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
2-hydroxymuconate semialdehyde
-
-
?
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
prepared from catechol
-
-
?
3-methylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol
-
-
?
3-methylcatechol ring-fission product + H2O
?
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol
-
-
?
catechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol
-
-
?
catechol ring-fission product + H2O
?
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol
-
-
?
additional information
?
-
-
the non-inducible levels of the enzyme activity appears negligible for metabolic purposes
-
-
?
additional information
?
-
-
the non-inducible levels of the enzyme activity appears negligible for metabolic purposes
-
-
?
additional information
?
-
-
enzyme of salicylate oxidation pathway
-
-
?
additional information
?
-
-
can not hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
additional information
?
-
-
can not hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
additional information
?
-
-
no activity with (2E,4E)-2,4-dihydroxy-6-oxonona-2,4-dienedioic acid
-
-
-
additional information
?
-
Pseudomonas mandelii 7HK4
-
no activity with (2E,4E)-2,4-dihydroxy-6-oxonona-2,4-dienedioic acid
-
-
-
additional information
?
-
Pseudomonas mandelii DSM 107615
-
no activity with (2E,4E)-2,4-dihydroxy-6-oxonona-2,4-dienedioic acid
-
-
-
additional information
?
-
-
enzyme is part of the pathway for the catabolism of toluene and m-xylene and p-xylene
-
-
?
additional information
?
-
-
enzyme of meta-cleavage pathway for the metabolism of benzoic acids to Krebs-cycle intermediates
-
-
?
additional information
?
-
-
enzyme of the hydrolytic branch of the meta-cleavage pathway for the catabolism of catechol and alkyl-substituted catechols
-
-
?
additional information
?
-
-
can not hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
additional information
?
-
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
enzyme is part of the pathway for the catabolism of toluene and m-xylene and p-xylene
-
-
?
additional information
?
-
the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency
-
-
?
additional information
?
-
-
the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency
-
-
?
additional information
?
-
the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
metabolism of 2-hydroxymuconate 6-semialdehyde through HMS hydrolase is predominant compared to metabolism by HMS dehydrogenase
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
metabolism of 2-hydroxymuconate 6-semialdehyde through HMS hydrolase is predominant compared to metabolism by HMS dehydrogenase
-
?
additional information
?
-
-
the non-inducible levels of the enzyme activity appears negligible for metabolic purposes
-
-
?
additional information
?
-
-
the non-inducible levels of the enzyme activity appears negligible for metabolic purposes
-
-
?
additional information
?
-
-
enzyme of salicylate oxidation pathway
-
-
?
additional information
?
-
-
enzyme is part of the pathway for the catabolism of toluene and m-xylene and p-xylene
-
-
?
additional information
?
-
-
enzyme of meta-cleavage pathway for the metabolism of benzoic acids to Krebs-cycle intermediates
-
-
?
additional information
?
-
-
enzyme of the hydrolytic branch of the meta-cleavage pathway for the catabolism of catechol and alkyl-substituted catechols
-
-
?
additional information
?
-
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
enzyme is part of the pathway for the catabolism of toluene and m-xylene and p-xylene
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Fe2+, Ca2+, Cu2+, Mg2+, Mn2+, Co2+, Li2+, and Zn2+ have no effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
N-ethylmaleimide and p-chloromercuribenzoate show no significant effect
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2315
2-hydroxy-5-methylmuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
0.232
2-hydroxymuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
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
-
-
-
0.005
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol
-
-
-
0.122
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol
-
-
-
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
-
-
-
0.0073
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
150 mM phosphate, 25°C, pH 7.5
0.0073
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
150 mM phosphate buffer, at pH 7.5 and 25°C
0.0164
2-hydroxy-6-oxohepta-2,4-dienoate
recombinant enzyme, pH 7.5, 25°C
additional information
additional information
steady-state kinetic analysis
-
additional information
additional information
-
steady-state kinetic analysis
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.15
2-hydroxy-5-methylmuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
18.2
2-hydroxymuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
21
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
150 mM phosphate, 25°C, pH 7.5
21
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
150 mM phosphate buffer, at pH 7.5 and 25°C
36.53
2-hydroxy-6-oxohepta-2,4-dienoate
recombinant enzyme, pH 7.5, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
50
2-hydroxy-5-methylmuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
2200
2-hydroxy-6-oxohepta-2,4-dienoate
recombinant enzyme, pH 7.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.18
purified recombinant enzyme, substrate 2-hydroxy-5-methylmuconate-6-semialdehyde, pH 7.5, 25°C
28.4
purified recombinant enzyme, substrate 2-hydroxy-6-oxohepta-2,4-dienoate, pH 7.5, 25°C
3.87
purified recombinant enzyme, substrate 2-hydroxymuconate-6-semialdehyde, pH 7.5, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 60
-
full enzyme activity up to 20°C for 30 min, and ca. 80% between 30 and 50°C, almost completely inactivated above 60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pheD encoded in the phe lower operon of the TOU catabolic pathway
UniProt
brenda
gene pheD encoded in the phe lower operon of the TOU catabolic pathway
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
DNA sequence analysis shows the gene order within the operons to be pheCDEFGHI (phe operon) and xyl-likeQKIH (xyl-like operon), identical to the order found for the isofunctional genes of meta operons in the toluene/xylene pathway of TOL plasmid pWW0 from Pseudomonas putida mt-2 and the phenol/methylphenol pathway of pVIl50 from Pseudomonas sp. CF600. The nucleotide and the deduced amino acid sequences are homologous to the equivalent gene and enzyme sequences from other Pseudomonas meta pathways, sequence analyses and homology studies
evolution
-
DNA sequence analysis shows the gene order within the operons to be pheCDEFGHI (phe operon) and xyl-likeQKIH (xyl-like operon), identical to the order found for the isofunctional genes of meta operons in the toluene/xylene pathway of TOL plasmid pWW0 from Pseudomonas putida mt-2 and the phenol/methylphenol pathway of pVIl50 from Pseudomonas sp. CF600. The nucleotide and the deduced amino acid sequences are homologous to the equivalent gene and enzyme sequences from other Pseudomonas meta pathways, sequence analyses and homology studies
-
metabolism
the hydrolytic branch of the TOU catabolic pathway involves direct formation of 2-hydroxypent-2,4-dienoate from the meta-cleavage product of catechol catalyzed by the enzyme. Catabolism of 3-methylcatechol and catechol through the hydrolytic branch and the oxalocrotonate branch, respectively, overview
metabolism
-
the hydrolytic branch of the TOU catabolic pathway involves direct formation of 2-hydroxypent-2,4-dienoate from the meta-cleavage product of catechol catalyzed by the enzyme. Catabolism of 3-methylcatechol and catechol through the hydrolytic branch and the oxalocrotonate branch, respectively, overview
-
additional information
genetic analysis of the Pseudomonas sp. OX1 TOU meta pathway involving the enzyme
additional information
-
genetic analysis of the Pseudomonas sp. OX1 TOU meta pathway involving the enzyme
additional information
-
genetic analysis of the Pseudomonas sp. OX1 TOU meta pathway involving the enzyme
-
Show AA Sequence and Transmembrane Helices (391 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
34400
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3 * 34400, isoenzyme HODHI, SDS-PAGE of 2-mercaptoethanol reduced enzyme
36700
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3 * 36700, isoenzyme HODHII, Alcaligenes eutrophus, SDS-PAGE of 2-mercaptoethanol reduced enzyme
30000
x * 30000, recombinant enzyme, SDS-PAGE, x * 31323.5, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
trimer
?
x * 30000, recombinant enzyme, SDS-PAGE, x * 31323.5, sequence calculation
?
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x * 30000, recombinant enzyme, SDS-PAGE, x * 31323.5, sequence calculation
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dimer
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2 * 31000-33000, SDS-PAGE after denaturation with 2-mercaptoethanol and urea
dimer
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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2 * 31000-33000, SDS-PAGE after denaturation with 2-mercaptoethanol and urea
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trimer
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3 * 34400, isoenzyme HODHI, SDS-PAGE of 2-mercaptoethanol reduced enzyme
trimer
-
3 * 36700, isoenzyme HODHII, Alcaligenes eutrophus, SDS-PAGE of 2-mercaptoethanol reduced enzyme
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A129V
A129V/I199V/V227I
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combination of mutations incompatible for correct folding
D224A
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aggregates into inclusion bodies and thus can not be purified
F104M
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mutation does not have any significant effect on enzyme characteristics
H252A
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aggregates into inclusion bodies and thus can not be purified
I199V
I199V/V2271
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combination of mutations incompatible for correct folding
S103A
V227I
A129V
A129V/I199V/V227I
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combination of mutations incompatible for correct folding
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I199V
I199V/V2271
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combination of mutations incompatible for correct folding
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S103A
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the mutant has 100000fold lower activity than that of the wild type enzyme
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V227I
D224A
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aggregates into inclusion bodies and thus can not be purified
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H252A
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aggregates into inclusion bodies and thus can not be purified
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S103A
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has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
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C254S
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1% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes
D65V
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activity below detection. Unstable, decreases in cellular extrects after 10 min
F108M
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18% of the activity of wild-type enzyme, enzyme displays greater thermostability than the wild-type enzyme
H249A
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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
H36A
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15% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
S152A
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80% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
A129V
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improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
A129V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate
I199V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
S103A
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has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
S103A
the mutant has 100000fold lower activity than that of the wild type enzyme
V227I
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
A129V
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improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
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A129V
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the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate
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I199V
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the kcat/Km value of the single mutant is higher than that of the wild type enzyme
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V227I
-
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
-
optimal stability at pH 7-8, rapid loss of activity below pH 5 and above pH 9.5
247052
7 - 9
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
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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
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isoenzyme HODHII is inactivated after 2 min, isoenzyme HODHI is inactivated after 4 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATCC 17707, strain 345, isozyme HODHII: TOL-like plasmid encoded enzyme, strain RA1012, isozyme HODHI: chromosomally-encoded enzyme
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recombinant enzyme from Escherichia coli strain JM109 by anion exchange chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
overexpression as an N-terminal His-tag from pSM12 in Escherichia coli BL21(DE3), or from plasmid pSM13 in Pseudomonas aeruginosa PAO1161
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
molecular biology
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orf234, encoding an alpha/beta hydrolase, which is distantly related to the meta-fission product hydrolases such as XylF, PhnD, and CumD
molecular biology
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the Pseudomonas strutzeri OX1 genes coding for toluene and o-xylene catabolism are organized into at least two operons, the one coding for the phenol catabolism displays a gene order similar to that of the Pseudomonas sp. strain CF600dmp operon, includes HMSH, and is coregulated by the tou operon activator TouR
molecular biology
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the Pseudomonas strutzeri OX1 genes coding for toluene and o-xylene catabolism are organized into at least two operons, the one coding for the phenol catabolism displays a gene order similar to that of the Pseudomonas sp. strain CF600dmp operon, includes HMSH, and is coregulated by the tou operon activator TouR
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molecular biology
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orf234, encoding an alpha/beta hydrolase, which is distantly related to the meta-fission product hydrolases such as XylF, PhnD, and CumD
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sala-Trepat, J.M.; Evans, W.C.
The meta cleavage of catechol by Azotobacter species. 4-Oxalocrotonate pathway
Eur. J. Biochem.
20
400-413
1971
Azotobacter vinelandii, Azotobacter vinelandii 206
brenda
Harayama, S.; Rekik, M.; Wasserfallen, A.; Bairoch, A.
Evolutionary relationships between catabolic pathways for aromatics: conservation of gene order and nucleotide sequences of catechol oxidation genes of pWW0 and NAH7 plasmids
Mol. Gen. Genet.
210
241-247
1987
Escherichia coli, Escherichia coli JM83
brenda
Horn, J.M.; Harayama, S.; Timmis, K.N.
DNA sequence determination of the TOL plasmid (pWW0) xylGFJ genes of Pseudomonas putida: implications for the evolution of aromatic catabolism
Mol. Microbiol.
5
2459-2474
1991
Pseudomonas putida
brenda
Diaz, E.; Timmis, K.N.
Identification of functional residues in a 2-hydroxymuconic semialdehyde hydrolase. A new member of the alpha/beta hydrolase-fold family of enzymes which cleaves carbon-carbon bonds
J. Biol. Chem.
270
6403-6411
1995
Pseudomonas putida
brenda
Nordlund, I.; Shingler, V.
Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600
Biochim. Biophys. Acta
1049
227-230
1990
Pseudomonas sp., Pseudomonas sp. CF 600
brenda
Bayly, R.C.; Diberardino, D.; Hughes, E.J.L.; Skurray, R.A.
The purification and properties of two isofunctional 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase from Alcaligenes eutrophus strain 345
J. Gen. Microbiol.
133
815-822
1987
Cupriavidus necator
-
brenda
Duggleby, C.J.; Williams, P.A.
Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (2-hydroxymuconic semialdehyde hydrolase) encoded by the TOL plasmid pWW0 from Pseudomonas putida mt-2
J. Gen. Microbiol.
132
717-726
1986
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
brenda
Aoki, K.; Kodama, N.; Murakami, S.; Shinke, R.
A high level of accumulation of 2-hydroxymuconic 6-semialdehyde from aniline by the transpositional mutant Y-2 of Pseudomonas species AW-2
Microbiol. Res.
152
129-135
1997
Pseudomonas sp., Pseudomonas sp. AW-2
brenda
Arenghi, F.L.; Berlanda, D.; Galli, E.; Sello, G.; Barbieri, P.
Organization and regulation of meta cleavage pathway genes for toluene and o-xylene derivative degradation in Pseudomonas stutzeri OX1
Appl. Environ. Microbiol.
67
3304-3308
2001
Pseudomonas stutzeri, Pseudomonas stutzeri OX1
brenda
Khajamohiddin, S.; Babu, P.S.; Chakka, D.; Merrick, M.; Bhaduri, A.; Sowdhamini, R.; Siddavattam, D.
A novel meta-cleavage product hydrolase from Flavobacterium sp. ATCC27551
Biochem. Biophys. Res. Commun.
351
675-681
2006
Flavobacterium sp., Flavobacterium sp. ATCC 27551
brenda
Jun, S.; Fushinobu, S.; Nojiri, H.; Omori, T.; Shoun, H.; Wakagi, T.
Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01
Biochim. Biophys. Acta
1764
1159-1166
2006
Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas fluorescens IP01
brenda
Betz, A.; Facey, S.J.; Hauer, B.; Tshisuaka, B.; Lingens, F.
Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Rue61a
J. Basic Microbiol.
40
7-23
2000
Arthrobacter sp., Arthrobacter sp. Rue61a
brenda
Saku, T.; Fushinobu, S.; Jun, J.S.; Ikeda, N.; Nojiri, H.; Yamane, H.; Omori, T.; Wakagi, T.
Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IPO1
J. Biosci. Bioeng.
93
568-574
2002
Pseudomonas fluorescens, Pseudomonas fluorescens IPO1
brenda
Bertini, L.; Cafaro, V.; Proietti, S.; Caporale, C.; Capasso, P.; Caruso, C.; Di Donato, A.
Deepening TOL and TOU catabolic pathways of Pseudomonas sp. OX1: cloning, sequencing and characterization of the lower pathways
Biochimie
95
241-250
2013
Pseudomonas sp. (G3KFX4), Pseudomonas sp., Pseudomonas sp. OX1 (G3KFX4)
brenda
Jun, S.Y.; Fushinobu, S.; Nojiri, H.; Omori, T.; Shoun, H.; Wakagi, T.
Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01
Biochim. Biophys. Acta
1764
1159-1166
2006
Pseudomonas fluorescens (P96965), Pseudomonas fluorescens IP01 (P96965), Pseudomonas fluorescens IP01
brenda
Saku, T.; Fushinobu, S.; Jun, S.; Ikeda, N.; Nojiri, H.; Yamane, H.; Omori, T.; Wakagi, T.
Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IP01
J. Biosci. Bioeng.
93
568-574
2002
Pseudomonas fluorescens (P96965), Pseudomonas fluorescens IP01 (P96965), Pseudomonas fluorescens IP01
brenda
Krikstaponis, A.; Meskys, R.
Biodegradation of 7-Hydroxycoumarin in Pseudomonas mandelii 7HK4 via ipso-hydroxylation of 3-(2,4-dihydroxyphenyl)-propionic acid
Molecules
23
2613
2018
Pseudomonas mandelii, Pseudomonas mandelii 7HK4, Pseudomonas mandelii DSM 107615
brenda
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