Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p).

@article{Hendle1995CrystallographicAE,
  title={Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p).},
  author={Jorg Hendle and Andrea Mattevi and Adrie H. Westphal and Jonne Spee and Aart de Kok and Alexey Teplyakov and Wim G. J. Hol},
  journal={Biochemistry},
  year={1995},
  volume={34 13},
  pages={4287-98}
}
Dihydrolipoamide acetyltransferase (E2p) is the structural and catalytic core of the pyruvate dehydrogenase multienzyme complex. In Azotobacter vinelandii E2p, residues Ser558, His610', and Asn614' are potentially involved in transition state stabilization, proton transfer, and activation of proton transfer, respectively. Three active site mutants, S558A, H610C, and N614D, of the catalytic domain of A. vinelandii E2p were prepared by site-directed mutagenesis and enzymatically characterized… CONTINUE READING
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