Two alpha-ketoglutarate-dependent dioxygenases carrying enantiospecific activity for the etherolytic cleavage of racemic phenoxypropionate herbicides [(RS)-2-(2,4-dichlorophenoxy)propionate and (RS)-2-(4-chloro-2-methylphenoxy)propionate] from Delftia acidovorans MC1 were characterized with respect to protein and sequence data. The (S)-phenoxypropionate/alpha-ketoglutarate-dioxygenase (SdpA) appeared as a monomeric enzyme with a molecular weight of 32 kDa in the presence of SDS. N-terminal sequences revealed relationship to alpha-ketoglutarate-dependent taurine dioxygenase (TauD) and to 2,4-dichlorophenoxyacetate/alpha-ketoglutarate-dioxygenase (TfdA). The (R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase (RdpA) referred to 36 kDa in the presence of SDS and to 108 kDa under native conditions. Internal sequences of fragments obtained after digestion made evident relationship to TfdA and TauD. Two-dimensional electrophoretic separation resulted in the resolution of up to 3 individual spots with almost identical molecular weights but different isoelectric points with both RdpA and SdpA. The structural differences of these isoenzyme forms are not yet clear.

中文翻译：

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产自Delftia acidovorans MC1蛋白的两种对映体特异性二氯丙醇/α-酮戊二酸双加氧酶和RdpA和SdpA的序列数据。

两种具有对映体特异性活性的α-酮戊二酸依赖性双加氧酶，用于外消旋苯氧基丙酸酯除草剂[（（RS）-2-（2,4-dichlorophenoxy）propionate和（RS）-2-（4-chloro-2-methylphenoxy）propionate]的醚解裂解。用蛋白质和序列数据表征了来自Delftia acidovorans MC1的]。（S）-苯氧基丙酸酯/α-酮戊二酸双加氧酶（SdpA）在SDS存在下以分子量为32 kDa的单体酶形式出现。N末端序列揭示了与α-酮戊二酸依赖性牛磺酸双加氧酶（TauD）和2,4-二氯苯氧乙酸酯/α-酮戊二酸双加氧酶（TfdA）的关系。（R）-苯氧基丙酸酯/α-酮戊二酸双加氧酶（RdpA）在SDS存在下为36 kDa，在自然条件下为108 kDa。消化后获得的片段的内部序列与TfdA和TauD具有明显的关系。二维电泳分离可分离多达3个分子量几乎相同的点，而RdpA和SdpA的等电点不同。这些同工酶形式的结构差异尚不清楚。