X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase

@article{Erskine1997XraySO,
  title={X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase},
  author={Peter T. Erskine and Natalie Senior and Sarah Awan and Richard H. Lambert and Gareth Lewis and Ian J. Tickle and Mohammed S. Sarwar and Paul Spencer and P. K. Thomas and Martin J. Warren and Peter M. Shoolingin-Jordan and Steve P. Wood and Jon B. Cooper},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={1025-1031}
}
5-Aminolaevulinate dehydratase (ALAD) is a homo-octameric metallo-enzyme that catalyses the formation of porphobilinogen from 5-aminolaevulinic acid. The structure of the yeast enzyme has been solved to 2.3 Å resolution, revealing that each subunit adopts a TIM barrel fold with a 39 residue N-terminal arm. Pairs of monomers wrap their arms around each other to form compact dimers and these associate to form a 422 symmetric octamer. All eight active sites are on the surface of the octamer and… CONTINUE READING

Similar Papers

Loading similar papers…