Arginine decarboxylase from Escherichia coli. IV. Structure of the pyridoxal phosphate binding site.

@article{Boeker1971ArginineDF,
  title={Arginine decarboxylase from Escherichia coli. IV. Structure of the pyridoxal phosphate binding site.},
  author={Elizabeth A. Boeker and Edmond H. Fischer and Esmond E. Snell},
  journal={The Journal of biological chemistry},
  year={1971},
  volume={246 22},
  pages={
          6776-81
        }
}
Abstract A total of three pyridoxyl-peptides were isolated from the inducible arginine decarboxylase of Escherichia coli B following reduction with NaBH4 and proteolysis with trypsin or chymotrypsin. Sodium borohydride reduces the Schiff base formed between pyridoxal-5'-P and the e-amino group of a lysyl residue of the protein. The sequence analysis of the three peptides is consistent with a unique pyridoxal-P binding site which has the structure Ala-Thr-His-Ser-Thr-His-(P-Pxy)Lys-Leu-Leu-Asn… CONTINUE READING

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