Amino acid sequence of proteinase K from the mold Tritirachium album Limber

The amino acid sequence of proteinase K (EC 3.4.21.14) from Tritirachium album Limber has been determined by analysis of fragments generated by cleavage with CNBr or BNPS‐skatole. The enzyme consists of a single peptide chain containing 277 amino acid residues, corresponding to M r 28 930. Comparison of the sequence with those of the serine proteinases reveals a high degree of homology (about 35%) to the subtilisin‐related enzyme. But in contrast to the subtilisins, proteinase K contains 2 disulfide bonds and a free cysteine residue. This finding may indicate that proteinase K is a member of a new subfamily of the subtilisins.

• Publication year

  1986

• Venue

  FEBS Letters

• Publication date

  1986-04-21

• Fields of study

  Biology, Materials Science, Chemistry

• Identifiers
  DOI 10.1016/0014-5793(86)80467-7
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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