The AMP-binding domain on adenylate kinase. Evidence for a conformational change during binary-to-ternary complex formation via photoaffinity labeling analyses.

@article{Pal1992TheAD,
  title={The AMP-binding domain on adenylate kinase. Evidence for a conformational change during binary-to-ternary complex formation via photoaffinity labeling analyses.},
  author={Pramod Kumar Pal and Zhengping Ma and Patrick S Coleman},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 35},
  pages={25003-9}
}
The topological location of the nucleotide substrate binding environments on adenylate kinase has been explored with the fluorescent molecule [4-benzoyl]benzoyl-1-amidofluorescein (BzAF) and the nucleotide analog 3'-O-[4-benzoyl]benzoyl-ATP (BzATP), which are site-directed photoaffinity probes that bind covalently at the individual nucleotide sites. The MgBzATP substituted for MgATP as a substrate for this enzyme, whereas BzAF, which is neither a substrate nor a nucleotide, behaved as a… CONTINUE READING

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