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Information on EC 1.14.11.44 - (R)-dichlorprop dioxygenase (2-oxoglutarate)
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EC Tree
1.14.11.44 (R)-dichlorprop dioxygenase (2-oxoglutarate)IUBMB Comments
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].
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Word Map
- 1.14.11.44
-
herbicide
-
aryloxyalkanoate
- maize
-
2,4-dichlorophenoxyacetic
-
aryloxyphenoxypropionate
- corn
- grain
-
near-isogenic
- carboxylase
-
quizalofop-p-ethyl
-
bacilliform
-
glyphosate-resistant
-
weed
-
agronomically
-
enantioselective
-
non-gm
-
herbicide-tolerant
- sugarcane
- accase
-
sphingobium
-
toxicological
-
non-transgenic
- ubiquitin
- auxin
- glyphosate
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
=
+
+
+
+
+
=
+
+
+
Synonyms
(R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase, 2-oxoglutarate-dependent (R)-dichlorprop dioxygenase, AAD-1, alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase, ariloxyalkanoate-dioxygenase-1, RdpA, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase
AAD-1
alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase
-
ariloxyalkanoate-dioxygenase-1
RdpA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + pyruvate + succinate + CO2
(2)
-
-
-
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2 = 4-chloro-2-methylphenol + pyruvate + succinate + CO2
(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].
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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
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
additional information
?
-
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
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
the enzyme catalyzes the initial step of microbial degradation of the chiral herbicide (R,S)-2-(2,4-dichlorophenoxy)propionate (R,S-dichlorprop)
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop. RdpA exclusively transforms the (R)-enantiomer of dichlorprop
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
-
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop. RdpA exclusively transforms the (R)-enantiomer of mecoprop
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop. RdpA exclusively transforms the (R)-enantiomer of mecoprop. The enzyme is specific for 2-oxoglutarate. Low levels of activity (1.9%) in presence of 2-oxoadipate. No activity with oxaloacetate, 2-oxobutyrate, and 2-oxovalerate
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
-
-
-
?
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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
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
i.e. (R)-dichlorprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH
-
-
?
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2
2,4-dichlorophenol + pyruvate + succinate + CO2
the enzyme catalyzes the initial step of microbial degradation of the chiral herbicide (R,S)-2-(2,4-dichlorophenoxy)propionate (R,S-dichlorprop)
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop, the enzyme is involved in degrading the chiral herbicides (RS)-2-(2,4-dichlorophenoxy)propionate (dichlorprop) and (RS)-2-(4-chloro-2-methylphenoxy)propionate (mecoprop). RdpA is highly specific for the cleavage of the R-configuration of dichlorprop and mecoprop
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
-
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
i.e. (R)-mecoprop, the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH
-
-
?
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2
4-chloro-2-methylphenol + pyruvate + succinate + CO2
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
ferrous iron is necessary for activity of the enzyme, and other divalent cations could not replace it
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-2-(4-chloro-2-methylphenoxy)propanoate
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
slightly reduced activity in the absence of ascorbate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.099
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C
0.108
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme F171A
0.38
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, wild-type enzyme
0.438
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme F171Q
1.55
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme R285A
2.3
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme V80A
2.8
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme Q93A
8.9
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme I106A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.87
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme R285A
2.9
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme F171A
3.38
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme F171Q
4
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme I106A
4.13
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme V80A
4.2
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, wild-type enzyme
4.33
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme Q93A
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme I106A
0.56
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme R285A
1.55
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme Q93A
1.8
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme V80A
7.7
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme F171Q
11
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, wild-type enzyme
26.9
(R)-2-(4-chloro-2-methylphenoxy)propanoate
pH 6.8, 30°C, mutant enzyme F171A
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
pH 6.0: about 60% of maximal activity, pH 7.5: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RDPA_SPHHM
Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / NBRC 16415 / MH)
295
0
33213
Swiss-Prot
-
A0A2S6TMY8_9PROT
299
0
34034
TrEMBL
-
A0A2S6U972_9PROT
246
0
27908
TrEMBL
-
A0A2S6UR65_9PROT
305
0
34936
TrEMBL
-
A0A2S6Q6L3_9PROT
281
0
32450
TrEMBL
-
A0A6J5GY81_9BURK
264
0
29692
TrEMBL
-
A0A2S6T7G1_9PROT
255
0
29224
TrEMBL
-
A0A2S6U2I1_9PROT
231
0
25283
TrEMBL
-
A0A2S6SVT4_9PROT
280
0
32443
TrEMBL
-
A0A2S6T2S4_9PROT
276
0
32020
TrEMBL
-
A0A2S6QEF9_9PROT
282
0
31876
TrEMBL
-
A0A2R8BD12_9RHOB
272
0
30047
TrEMBL
-
A0A2S6UHL6_9PROT
278
0
31083
TrEMBL
-
A0A2S6U1Q5_9PROT
296
0
33092
TrEMBL
-
A0A2S6TR69_9PROT
282
0
32028
TrEMBL
-
A0A2S6TE18_9PROT
282
0
31987
TrEMBL
-
A0A2S6Q683_9PROT
291
0
32786
TrEMBL
-
A0A2S6SEY6_9PROT
280
0
32443
TrEMBL
-
A0A2S6USD6_9PROT
259
0
30074
TrEMBL
-
A0A2S6TIY1_9PROT
280
0
31565
TrEMBL
-
A0A2S6TQ80_9PROT
295
0
33174
TrEMBL
-
A0A2S6QEF0_9PROT
301
0
33945
TrEMBL
-
A0A2S6TJZ1_9PROT
289
0
32834
TrEMBL
-
A0A2S6S886_9PROT
280
0
32216
TrEMBL
-
A0A2P2E6X3_9PROT
273
0
30431
TrEMBL
-
A0A2S6SHI1_9PROT
276
0
32034
TrEMBL
-
A0A2S6S469_9PROT
281
0
32267
TrEMBL
-
A0A2S6QNK7_9PROT
278
0
32304
TrEMBL
-
A0A2S6TIR0_9PROT
288
0
31782
TrEMBL
-
A0A2S6SJS8_9PROT
275
0
31807
TrEMBL
-
A0A2S6U212_9PROT
283
0
31328
TrEMBL
-
A0A2S6U356_9PROT
290
0
32475
TrEMBL
-
A0A2S6QDE5_9PROT
279
0
31795
TrEMBL
-
A0A644XW05_9ZZZZ
291
0
32729
TrEMBL
other Location (Reliability: 2)
A0A2S6QEL0_9PROT
294
0
33953
TrEMBL
-
A0A2P5VLK9_9PROT
279
0
31522
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F171A
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
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
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
exhibits 0.7% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
I106G/G107N
exhibits 8.7% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
L83A
exhibits about 10% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
Q93A
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
V80A
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
R285A
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
R285A
exhibits about 10% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
Y221A
exhibits 5.2% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
Y221A
exhibits about 10% of wild-type enzyme activity with (R)-2-(4-chloro-2-methylphenoxy)propanoate
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His6-tagged fusion protein from Escherichia coli BL21(DE3)(pLysS)
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Müller, T.A.; Fleischmann, T.; van der Meer, J.R.; Kohler, H.P.
Purification and characterization of two enantioselective alpha-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH
Appl. Environ. Microbiol.
72
4853-4861
2006
Sphingobium herbicidovorans (Q8KSC8), Sphingobium herbicidovorans
brenda
Paulin, M.M.; Nicolaisen, M.H.; Sorensen, J.
Abundance and expression of enantioselective rdpA and sdpA dioxygenase genes during degradation of the racemic herbicide (R,S)-2-(2,4-dichlorophenoxy)propionate in soil
Appl. Environ. Microbiol.
76
2873-2883
2010
Sphingobium herbicidovorans (Q8KSC8)
brenda
Westendorf, A.; Benndorf, D.; Müller, R.H.; Babel, W.
The two enantiospecific dichlorprop/alpha-ketoglutarate-dioxygenases from Delftia acidovorans MC1 - protein and sequence data of RdpA and SdpA
Microbiol. Res.
157
317-322
2002
Delftia acidovorans (P83310), Delftia acidovorans, Delftia acidovorans MC1 (P83310), Delftia acidovorans MC1
brenda
Müller, T.A.; Zavodszky, M.I.; Feig, M.; Kuhn, L.A.; Hausinger, R.P.
Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/alpha-ketoglutarate dioxygenases
Protein Sci.
15
1356-1368
2006
Sphingobium herbicidovorans (Q8KSC8)
brenda
Queiroz, A.; Vidal, R.
The development of dichlorophenoxyacetate herbicide tolerant crops Literature review
Planta Daninha
32
649-654
2014
Sphingobium herbicidovorans (Q8KSC8), Sphingobium herbicidovorans MH (Q8KSC8)
-
brenda
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