Information on EC 1.14.11.44 - (R)-dichlorprop dioxygenase (2-oxoglutarate)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.44
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RECOMMENDED NAME
GeneOntology No.
(R)-dichlorprop dioxygenase (2-oxoglutarate)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-(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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(R)-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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SYSTEMATIC NAME
IUBMB Comments
((R)-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 (R)-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
(R)-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
(R)-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+
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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-(4-chloro-2-methylphenoxy)propanoate
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Q93A variant retains 60% of wild-type enzyme activity, but this drops to 35% when the racemate is provided, suggesting that Gln93 prevents the incorrect enantiomer from binding to and inhibiting the enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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slightly reduced activity in the absence of ascorbate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.164
(R)-(2,4-dichlorophenoxy)propanoate
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pH 6.8, 30C
0.099 - 8.9
(R)-2-(4-chloro-2-methylphenoxy)propanoate
0.003
2-oxoglutarate
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pH 6.8, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.87 - 4.33
(R)-2-(4-chloro-2-methylphenoxy)propanoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45 - 26.9
(R)-2-(4-chloro-2-methylphenoxy)propanoate
4190
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 60% of maximal activity, pH 7.5: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 5.9
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104000
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gel filtration
108000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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stable for up to 7 days
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by several freezing and thawing cycles
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for up to 8 weeks
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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 rdpA 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
F171A
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exhibits about 70% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 245% compared to the wild-type value
F171Q
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exhibits about 70% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 70% compared to the wild-type value
I106A
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exhibits about 30% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 5% compared to the wild-type value
I106G/G107I
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exhibits 0.7% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
I106G/G107N
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exhibits 8.7% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
L83A
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exhibits about 10% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
Q93A
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exhibits about 60% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 14% compared to the wild-type value
R285A
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exhibits 14.8% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 5% compared to the wild-type value; exhibits about 10% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
V80A
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exhibits about 60% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate. kcat/Km is 17% compared to the wild-type value
Y221A
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exhibits 5.2% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate; exhibits about 10% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate