Information on EC 1.14.11.43 - (S)-dichlorprop dioxygenase (2-oxoglutarate)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.43
-
RECOMMENDED NAME
GeneOntology No.
(S)-dichlorprop dioxygenase (2-oxoglutarate)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + pyruvate + succinate + CO2
show the reaction diagram
(2)
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-
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(S)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2 = 4-chloro-2-methylphenol + pyruvate + succinate + CO2
show the reaction diagram
(1)
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-
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SYSTEMATIC NAME
IUBMB Comments
(S)-2-(4-chloro-2-methylphenoxy)propanoate,2-oxoglutarate:oxygen oxidoreductase (pyruvate-forming)
Fe2+-dependent enzyme. The enzymes from the Gram-negative bacteria Delftia acidovorans MC1 and Sphingomonas herbicidovorans MH are involved in the degradation of the (S)-enantiomer of the phenoxyalkanoic acid herbicides mecoprop and dichlorprop [1,2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
show the reaction diagram
i.e. (S)-dichlorprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH. SdpA activity is completely absent in the absence of 2-oxoglutarate
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-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
2-methyl-4-chlorophenol + pyruvate + succinate + CO2
show the reaction diagram
i.e. (S)-mecoprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH. SdpA activity is completely absent in the absence of 2-oxoglutarate
-
-
?
(S)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
show the reaction diagram
(S)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
show the reaction diagram
additional information
?
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construction of homology models of SdpA and RdpA from Sphingomonas herbicidovorans MH and the use of docking to identify residues likely to be involved in herbicide binding
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-
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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
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
show the reaction diagram
Q700X4
i.e. (S)-dichlorprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH. SdpA activity is completely absent in the absence of 2-oxoglutarate
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-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
2-methyl-4-chlorophenol + pyruvate + succinate + CO2
show the reaction diagram
Q700X4
i.e. (S)-mecoprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH. SdpA activity is completely absent in the absence of 2-oxoglutarate
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-
?
(S)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
show the reaction diagram
(S)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
ferrous iron is necessary for activity of the enzyme and other divalent cations could not replace it
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-2-(2,4-dichlorophenoxy)propanoate
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slight inhibition
(S)-2-(4-chloro-2-methylphenoxy)propanoate
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slight inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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slightly reduced in the absence of ascorbate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.495
(S)-(2,4-dichlorophenoxy)propanoate
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pH 6.8, 30C
0.091 - 2.9
(S)-2-(4-chloro-2-methylphenoxy)propanoate
0.0196
2-oxoglutarate
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pH 6.8, 30C
0.159
O2
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pH 6.8, 30C, above 0.23 mM
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35 - 16.83
(S)-2-(4-chloro-2-methylphenoxy)propanoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 104.5
(S)-2-(4-chloro-2-methylphenoxy)propanoate
5447
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
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pH 6.0: about 30% of maximal activity, pH 7.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
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20C: about 40% of maximal activity, 35-40C: optimal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 6.3
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23700
gel filtration
33700
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1 * 33700, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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stable for several hours
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
storage on ice and freeze-thaw cycles reduce the activity to about 80% of the original activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 3 days, less than 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His6-tagged fusion protein from Escherichia coli BL21(DE3)(pLysS)
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expression of sdpA in Delftia acidovorans
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
rdpA and sdpA gene expression is constitutive at a basal level but is induced in response to (R,S)-dichlorprop degradation under in situ conditions
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E69A
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exhibits 30.8% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 42% compared to the wild-type value
G97I/N98G
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exhibits 3.8% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 0.6% compared to the wild-type value
G97N/N98G
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exhibits 0.3% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate
H208A
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exhibits about 1.4% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 0.1% compared to the wild-type value
H272A
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exhibits about 1.2% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate
Q162F
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exhibits about 4.8% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate
R207A
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exhibits about 17.3% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 2% compared to the wild-type value
R207V
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exhibits about 2.8% of wild-type enzyme activity with (S)-2-(4-chloro-2-methylphenoxy)propanoate
R274A
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inactive mutant enzyme