Proteinase

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Proteinase (PRO) are enzymes which hydrolyze peptide bonds. They are classified by the amino acid site of their cleavage or by the pH at which they are active.

  • PRO B is a serine protease. For more details see Streptomyces griseus proteinase B.
  • PRO A is a carboxylproteinase.
  • PRO K is a serine protease which cleaves proteins preferentially after hydrophobic residues. Calcium ions contribute to the stability of the enzyme. PRO K is active over a wide pH range and is used in molecular biology to inactivate nucleases from preparations of DNA or RNA. PRO K is used in the partial proteolysis of lactoferrin into its N- and C-lobe. The two lobes of lactoferrin have different antimicrobial and antifungal properties. PRO K can digest hair (keratin).

E. coli proteinase K (grey) complex with lactoferrin peptide (green) and Ca+2 (green) and nitrate ions (PDB code 2duj)

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3D structures of proteinase3D structures of proteinase

Updated on 21-May-2015

ReferencesReferences

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Karsten Theis