Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila.

@article{Gorrell2005StructuralAK,
  title={Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila.},
  author={Andrea Gorrell and Sarah H. Lawrence and James G. Ferry},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 11},
  pages={10731-42}
}
Acetate kinase catalyzes transfer of the gamma-phosphate of ATP to acetate. The only crystal structure reported for acetate kinase is the homodimeric enzyme from Methanosarcina thermophila containing ADP and sulfate in the active site (Buss, K. A., Cooper, D. C., Ingram-Smith, C., Ferry, J. G., Sanders, D. A., and Hasson, M. S. (2001) J. Bacteriol. 193, 680-686). Here we report two new crystal structure of the M. thermophila enzyme in the presence of substrate and transition state analogs. The… CONTINUE READING

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