Structure-function relationships in Escherichia coli adenylate cyclase.

@article{Linder2008StructurefunctionRI,
  title={Structure-function relationships in Escherichia coli adenylate cyclase.},
  author={J{\"u}rgen Ulrich Linder},
  journal={The Biochemical journal},
  year={2008},
  volume={415 3},
  pages={
          449-54
        }
}
Class I adenylate cyclases are found in gamma- and delta-proteobacteria. They play central roles in processes such as catabolite repression in Escherichia coli or development of full virulence in pathogens such as Yersinia enterocolitica and Vibrio vulnificus. The catalytic domain (residues 2-446) of the adenylate cyclase of E. coli was overexpressed and purified. It displayed a V(max) of 665 nmol of cAMP x mg(-1) x min(-1) and a K(m) of 270 microM. Titration of the metal cofactor Mg(2… CONTINUE READING

References

Publications referenced by this paper.

Mechanism of Escherichia coli adenylate cyclase

  • L. Aravind, E. V. Koonin
  • 1999

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