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].
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The enzyme appears in viruses and cellular organisms
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].
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
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
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
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
i.e. (S)-mecoprop. SdpA is specific for the (S) enantiomer. 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
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
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
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
i.e. (S)-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). SdpA is highly specific for the cleavage of the S-configuration of dichlorprop and mecoprop
Mller, 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
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