Dipeptide seryl-histidine and related oligopeptides cleave DNA, protein, and a carboxyl ester.

@article{Li2000DipeptideSA,
  title={Dipeptide seryl-histidine and related oligopeptides cleave DNA, protein, and a carboxyl ester.},
  author={Yuesheng Li and Yufen Zhao and Scott Hatfield and Rong Wan and Qingzhang Zhu and Xiaona Li and Mark Chad McMills and Yuliang Ma and Jinglan Li and Kenneth L B Brown and Cui-cui He and Fengyu Liu and Xiaozhuo Chen},
  journal={Bioorganic & medicinal chemistry},
  year={2000},
  volume={8 12},
  pages={
          2675-80
        }
}
The amino acids histidine (His) and serine (Ser), or amino acids similar to Ser, function together as key catalytic amino acids in the active sites of such diverse enzymes as the serine- and thiol-proteases, lipases, and esterases. Ser and His are also conserved in the intein-extein junctions of the phylogenetically widespread self-splicing proteins and at the N- and C-termini of the homing endonucleases spliced from them. Here we show that the dipeptide seryl-histidine (Ser-His) and related… CONTINUE READING
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