Enzymatic hydrolysis of enterochelin and its iron complex in Escherichia Coli K-12. Properties of enterochelin esterase.

@article{Greenwood1978EnzymaticHO,
  title={Enzymatic hydrolysis of enterochelin and its iron complex in Escherichia Coli K-12. Properties of enterochelin esterase.},
  author={K T Greenwood and Richard K J Luke},
  journal={Biochimica et biophysica acta},
  year={1978},
  volume={525 1},
  pages={209-18}
}
Properties of the enzyme which hydrolyses enterochelin (a cyclic trimer of 2,3-dihydroxy-N-benzoyl-L-serine) to 2,3-dihydroxybenzoylserine have been investigated with a view to resolving discrepancies between earlier reports. Enterochelin esterase, previously reported to consists of two components (O'Brien, I.G., Cox, G.B. and Gibson, F. (1971) Biochim. Biophys. Acta 237, 537-549), has been shown to be fully active in the absence of the so-called A component. The hydrolase described previously… CONTINUE READING

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