Cobalt(III) affinity-labeled aspartokinase. Formation of substrate and inhibitor adducts.

@article{Wright1976CobaltIIIAA,
  title={Cobalt(III) affinity-labeled aspartokinase. Formation of substrate and inhibitor adducts.},
  author={J. K. Wright and J. Feldman and M. Takahashi},
  journal={Biochemistry},
  year={1976},
  volume={15 17},
  pages={
          3704-10
        }
}
The kinase active site of the aspartokinase-homoserine dehydrogenase enzyme complex of Excherichia coli has been affinity labeled both with substrates aspartate and adenosine triphosphate and feedback inhibitor threonine. Co(III) exchange-inert adducts of aspartokinase and inhibitor or substrates were produced in situ by oxidation of Co(II) with H2O2. Emzyme-Co(III)-adenosine 5'-triphosphate (ATP), enzyme-Co(III)-aspartate, and enzyme-Co(III)-threonine ternary adducts were produced in this… Expand
Kinetic and magnetic properties of cobalt(III) ion in the active site of carbonic anhydrase.
Cobalt(III) labeling of methionyl-tRNA synthetase from Escherichia coli.
...
1
2
...

References

SHOWING 1-10 OF 25 REFERENCES
Cobalt(III), a probe of metal binding sites of Escherichia coli alkaline phosphatase.
  • R. Anderson, B. Vallee
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1975
Cobalt (3) carboxypeptidase A: preparation and esterase activity.
...
1
2
3
...