Proteinase: Difference between revisions
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<StructureSection load='' size='350' side='right' scene='Journal:JBSD:39/Cv/11' caption=''> | <StructureSection load='' size='350' side='right' scene='Journal:JBSD:39/Cv/11' caption=''> | ||
'''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 see [[Streptomyces griseus proteinase B]].<br /> | * '''PRO B''' is a serine protease<ref>PMID:3325823</ref>. For more details see [[Streptomyces griseus proteinase B]].<br /> | ||
* '''PRO A''' is a carboxylproteinase.<br /> | * '''PRO A''' is a carboxylproteinase<ref>PMID:6799292</ref>.<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<ref>PMID:9606141</ref>. 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). | ||
=== The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen-bond density in the reactive loop <ref>doi 10.1080/07391102.2012.745378</ref> === | === The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen-bond density in the reactive loop <ref>doi 10.1080/07391102.2012.745378</ref> === | ||