The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction.

@article{Jaggi1997TheTO,
  title={The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction.},
  author={R Jaggi and Wally C van Heeswijk and Hans V. Westerhoff and David L. Ollis and Subhash G. Vasudevan},
  journal={The EMBO journal},
  year={1997},
  volume={16 18},
  pages={5562-71}
}
Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1-423 (AT-N… CONTINUE READING

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References

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The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli

W. C. van Heeswijk, M. Rabenberg, H. V. Westerhoff, D. Kahn
Mol. Microbiol., • 1993
View 7 Excerpts
Highly Influenced

DNA polymerase beta belongs to an ancient nucleotidyltransferase superfamily.

Trends in biochemical sciences • 1995
View 1 Excerpt
Highly Influenced

X - ray structure of the signal transducing protein PII 8690 – 8695 . from Escherichia coli at 1 . 9 Å

P. Z. Smyrniotis, E. Cheah, +3 authors N. E. Dixon
1996

Structure of the Escherichia coli signal transducing of Escherichia coli glutamine synthetase

M. Rabenberg, H. V. Westerhoff, +3 authors C. Schneider
Anal . Biochem . • 1994

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