Evolution of quaternary structure in a homotetrameric enzyme.

  title={Evolution of quaternary structure in a homotetrameric enzyme.},
  author={M. D. W. Griffin and Renwick C J Dobson and Frederick Grant Pearce and Laurence Antonio and Andrew E. Whitten and Chu Kong Liew and Joel P. Mackay and Jill Trewhella and Geoffrey B Jameson and Matthew A. Perugini and Juliet A Gerrard},
  journal={Journal of molecular biology},
  volume={380 4},
Dihydrodipicolinate synthase (DHDPS) is an essential enzyme in (S)-lysine biosynthesis and an important antibiotic target. All X-ray crystal structures solved to date reveal a homotetrameric enzyme. In order to explore the role of this quaternary structure, dimeric variants of Escherichia coli DHDPS were engineered and their properties were compared to those of the wild-type tetrameric form. X-ray crystallography reveals that the active site is not disturbed when the quaternary structure is… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.


Publications citing this paper.
Showing 1-10 of 26 extracted citations


Publications referenced by this paper.
Showing 1-10 of 46 references

Effect of fadR gene knockout on the metabolism of Escherichia coli based on analyses of protein expressions, enzyme activities and intracellular metabolite concentrations

L. F. Peng, K. Shimizu
Enzyme Microb. Technol • 2006
View 1 Excerpt

Similar Papers

Loading similar papers…