Specificity has been demonstrated in that the phenylacetyltransferase protein exhibits activity towards phenylacetyl-CoA, phenoxyacetyl-CoA and 2,4-D, but not 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), whereas the benzoyltransferase protein conjugates both 2,4-D and 2,4,5-T [37]. Interestingly, the high Km values for glycine (100 – 1000 mM) for both phenoxyherbicide-CoAs by either of the bovine mitochondrial N-acyltransferases and slow catalytic rate constants are characteristic of alternate substrate inhibitors [37].
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