Biopolym. Cell. 2001; 17(6):512-521.
http://dx.doi.org/10.7124/bc.0005D9
Structure and Function of Biopolymers
Revision of Penicillium vitale catalase amino acid sequence. Reconstruction of polypeptide chain
1Kozlov E. A., 1Levitina T. L., 1Bobrovskaja M. T., 1Ovander M. N., 1Gudkova L. V., 1Latishko N. V., 1Radomskiy N. F.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

The complete amino acid sequence of P. vitale catalase comprised of 689 amino acid residues was reconstructed from 45 peptides and fragments published earlier. The sequences 1–162 and 314–573 were reconstructed by means of overlapping of peptides and fragments sequences. The sequences 163–313 and 574–689 were reconstructed by means of comparison of the peptides and fragments sequences with the P. vitale ami/to acid sequence established by X-ray method. The primary structures of 6 long catalases from two taxonomic groups (fungus, bacteria) containing additional C-terminal domain have been compared. The matrix of the catalases and their C-terminat domains «alliance» was constructed.
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References

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