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

@article{Jany1986AminoAS,
  title={Amino acid sequence of proteinase K from the mold Tritirachium album Limber},
  author={K D Jany and Georg Lederer and B. Mayer},
  journal={FEBS Letters},
  year={1986},
  volume={199}
}
Proteinase K from Tritirachium album Limber. Characterization of the chromosomal gene and expression of the cDNA in Escherichia coli.
TLDR
The nucleotide-sequence analysis of the gene and its flanking regions has revealed that the proteinase-K gene is composed of two exons and one 63-bp-long intron located in the proregion, and a putative promoter sequence and a capping site have been identified, suggesting that the transcription-start site is located 103-bp upstream of the ATG initiation codon.
Purification and characterization of a serine proteinase from senescent sporophores of the commercial mushroom Agaricus bisporus.
TLDR
A proteinase has been purified from the stipes of senescent sporophores of the mushroom Agaricus bisporus and has similar properties to, and 60% N-terminal sequence identity with, proteinase K from the fungus Tritirachium album.
Cloning and sequencing of the alkaline extracellular protease gene of Yarrowia lipolytica
The XPR2 gene encoding an alkaline extracellular protease (AEP) from Yarrowia lipolytica was cloned, and its complete nucleotide sequence was determined. The amino acid sequence deduced from the
Improving the catalytic performance of Proteinase K from Parengyodontium album for use in feather degradation.
A cold-adapted extracellular serine proteinase of the yeast Leucosporidium antarcticum
TLDR
The proteinase lap2 is the first psychrophilic subtilase in this family and has homology with subtilases of the proteinase K subfamily (clan SB, family S8, subfamily C).
Properties of a subtilisin-like proteinase from a psychrotrophic Vibrio species comparison with proteinase K and aqualysin I.
TLDR
The stability of the Vibrio proteinase was found to be significantly lower than of either proteinase K or aqualysin I, and the order of reactivity observed in these reactions most likely reflects the accessibility of the reactive cystine or methionine side chains present in the three related proteinases, and hence a difference in the compactness of their protein structures.
A basic serine protease from Paecilomyces lilacinus with biological activity against Meloidogyne hapla eggs.
TLDR
It can be concluded that the serine protease might play a role in penetration of the fungus through the egg-shell of nematodes.
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References

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Crystallization of the fungal enzyme proteinase K and amino acid composition.
Proteinase K from Tritirachium album Limber.
TLDR
The nucleotide-sequence analysis of the gene and its flanking regions has revealed that the proteinase-K gene is composed of two exons and one 63-bp-long intron located in the proregion, and a putative promoter sequence and a capping site have been identified, suggesting that the transcription-start site is located 103-bp upstream of the ATG initiation codon.
Proteinase K from Tritirachium album limber. I. Molecular mass and sequence around the active site serine residue.
TLDR
From the determined sequences it is concluded that the fungal proteinase K is phylogenetically related to the bacterial subtilisins.
Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin.
TLDR
Proteinase K is the second enzyme in this family of serine proteases to be studied by X‐ray diffraction, thus confirming the existence of two unrelated families of serines proteases in pro‐and eukaryotes.
The sequence determination of a protein in a micro scale: the sequence analysis of ribosomal protein L34 of Escherichia coli.
  • R. Chen
  • Biology, Chemistry
    Hoppe-Seyler's Zeitschrift fur physiologische Chemie
  • 1976
TLDR
The complete amino acid sequence of ribosomal protein L34 has been established by improved micro techniques with 3 mg of the lyophilized protein by the combined micro dansyl-Edman technique.
Determination of the complete amino-acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN', Carlsberg and amylosacchariticus.
TLDR
The amino-acid replacement analysis of the four subtilisins leads to the conclusion that they have evolved almost independently, suggesting that these molecules have had a common ancestral precursor.
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