Information on EC 4.2.1.83 - 4-oxalomesaconate hydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.83
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RECOMMENDED NAME
GeneOntology No.
4-oxalomesaconate hydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
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gallate degradation I
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gallate degradation II
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methylgallate degradation
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Microbial metabolism in diverse environments
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protocatechuate degradation I (meta-cleavage pathway)
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SYSTEMATIC NAME
IUBMB Comments
(1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate 1,2-hydro-lyase (2-hydroxy-4-oxobutane-1,2,4-tricarboxylate-forming)
This enzyme participates in the degradation of protocatechuate (via the meta-cleavage pathway), syringate and gallate, catalysing the reaction in the opposite direction [1-3]. It accepts the enol-form of 4-oxalomesaconate, 2-hydroxy-4-carboxy-hexa-2,4-dienedioate [4].
CAS REGISTRY NUMBER
COMMENTARY hide
85204-95-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pmdE
UniProt
Manually annotated by BRENDA team
gene pmdE
UniProt
Manually annotated by BRENDA team
gene pmdE
UniProt
Manually annotated by BRENDA team
strain NGJ1
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-3-carboxy-5-oxo-2-hexenedioic acid + H2O
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
show the reaction diagram
2-hydroxy-4-carboxy-hexa-2,4-dienedioate
4-carboxy-4-hydroxy-2-oxoadipate + H2O
show the reaction diagram
4-oxalomesaconate
?
show the reaction diagram
additional information
?
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enzyme is essential for catabolism of both vanillate and syringate
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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
additional information
?
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Q9KWL6
enzyme is essential for catabolism of both vanillate and syringate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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PocOMH possesses one Zn2+ per subunit. It strongly binds to the enzyme protein
additional information
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no Fe2+- or Mn2+-dependent activation in the presence of DTT under anaerobic conditions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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inhibition is primarily due to modification of Cys186. DTNB-treated C186S remains fully active
HgCl2
iodoacetamide
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weak
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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cysteine
reduced glutathione
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0064 - 0.138
(E)-3-Carboxy-5-oxo-2-hexenedioic acid
0.014
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
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pH 8.0, 24°C
0.0029 - 0.087
4-oxalomesaconate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 159
4-oxalomesaconate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 9.6
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50% of activity maximum at pH 7.2 and 9.6
7.4 - 9.1
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50% of activity maximum at pH 7.4 and 9.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
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focusing at 6°C
5.81
sequence calculation
6.23
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
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2 * 37000, SDS-PAGE
55000
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gel filtration
68000
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gel filtration
69500
gel filtration
72000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is unstable in absence of reducing reagents
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678816
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme gradually inactivated, complete loss of activity after 6 months
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-20°C, stable for at least 1 month
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-25°C, 20 mM potassium phosphate buffer containing 1 mM DTT, stable for at least 2 months
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4°C, 20 mM potassium phosphate buffer containing 1 mM DTT, wild-type enzyme loses 20% of initial activity after 1 d
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene pmdE; gene pmdE, expression of wild-type and mutants in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C124S
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kcat/Km for 4-oxalomesaconate is 1.9fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C131S
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kcat/Km for 4-oxalomesaconate is 26% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C183S
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kcat/Km for 4-oxalomesaconate is 1.8fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C186S
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kcat/Km for 4-oxalomesaconate is 16% higher than wild-type value, mutant enzyme is more stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C205S
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kcat/Km for 4-oxalomesaconate is 29% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C260S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C92S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C96S
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kcat/Km for 4-oxalomesaconate is 3.9fold lower than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C131S
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kcat/Km for 4-oxalomesaconate is 26% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C183S
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kcat/Km for 4-oxalomesaconate is 1.8fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C260S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C92S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C96S
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kcat/Km for 4-oxalomesaconate is 3.9fold lower than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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additional information
Show AA Sequence (104 entries)
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