Proteinase: Difference between revisions

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

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 <StructureSection load='2duj' size='340' side='right' caption='E. coli proteinase K (grey) complex with lactoferrin peptide (green) and Ca+2 (green) and nitrate ions (PDB code [[2duj]])' scene=''>
-'''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 on PRO B 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).
+'''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.<br />
+*  '''PRO B''' is a serine protease.  For more details on PRO B see [[Streptomyces griseus proteinase B]].<br />
+*  '''PRO A''' is a carboxylproteinase.<br />
+*  '''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).
 ==3D structures of proteinase==