Proteinase: Difference between revisions
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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=''> | <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.<br /> | '''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 | * '''PRO B''' is a serine protease. For more details see [[Streptomyces griseus proteinase B]].<br /> | ||
* '''PRO A''' is a carboxylproteinase.<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). | * '''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). | ||