Amino acid sequence and S-S bonds of Penicillium brevicompactum guanyl-specific ribonuclease

FEBS Lett. 1984 Nov 19;177(2):246-8. doi: 10.1016/0014-5793(84)81292-2.

Abstract

The primary structure of Penicillium brevicompactum guanyl-specific RNase was determined. The enzyme consists of 102 amino acid residues, Mr 10801. The 4 cysteine residues of the RNase are linked in pairs by disulfide bonds: Cys2-Cys10, Cys6-Cys101. P. brevicompactum RNase structure is similar to RNase T1; the degree of homology is 66%.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Disulfides / analysis
  • Endoribonucleases*
  • Penicillium / enzymology*
  • Peptide Fragments / analysis
  • Ribonuclease T1*

Substances

  • Disulfides
  • Peptide Fragments
  • Endoribonucleases
  • Ribonuclease T1