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='' size='350' side='right' scene='Journal:JBSD:39/Cv/11' caption=''>
__TOC__
==Function==
 
'''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).<br />
*'''Endothiapepsin''' is an '''aspartic PRO''' from ''Cryphonectria parasitica''<ref>PMID:1525155</ref>.<br />
*'''Saccharopepsin''' is an '''aspartic PRO''' from yeast<ref>PMID:17447722</ref>.<br />
*'''Falcipain''' is an '''cystein PRO''' from ''Plasmodium falciparum''<ref>PMID:21660657</ref>.<br />
For '''cysteine PRO''' from ''Trypanosoma cruzi'' see [[Cruzain]].


==3D structures of proteinase==
==3D structures of proteinase==
[[Proteinase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
 
===PRO A===
 
[[2sga]] – SgPRO – ''Streptomyces griseus''<br />
[[2jxr]], [[1fmu]], [[1fmx]] – yPRO - yeast<br />
[[1sgc]] - SgPRO + chymostatin A<br />
[[3sga]], [[4sga]], [[5sga]] - SgPRO + polypeptide inhibitor<br />
[[1dp5]], [[1dpj]], [[1g0v]] - yPRO + polypeptide inhibitor IA3<br />
[[1fq5]] - yPRO + inhibitor
 
===PRO B===
 
[[3sgb]] – SgPRO + turkey ovomucoid inhibitor<br />
[[1sgp]], [[1sgq]], [[1sgr]], [[1cso]], [[1ct0]], [[1ct2]], [[1ct4]], [[1ds2]], [[2sgp]], [[2nu3]], [[2nu4]] – SgPRO + turkey ovomucoid inhibitor (mutant)<br />
[[4sgb]] - SgPRO + potato inhibitor
 
===PRO K===
 
[[2prk]], [[1cnm]], [[1egq]], [[2id8]], [[2g4v]], [[2v8b]], [[3gt3]], [[3gt4]], [[3d9q]], [[3ddz]], [[3de0]] , [[3de1]], [[3de2]], [[3de3]], [[3de4]], [[3de5]], [[3de6]], [[3de7]], [[3dvq]], [[3dvr]], [[3dvs]], [[3dw1]], [[3dw3]], [[3dwe]], [[3i2y]], [[3i30]], [[3i37]], [[3i34]], [[3l1k]], [[3aj8]], [[3aj9]], [[3q40]], [[3q5g]], [[3qmp]], [[4b5l]], [[4fon]] – EaPRO + Ca – ''Engyodontium album'' <br />
[[1ic6]] – EaPRO (mutant) + Ca  <br />
[[1ptk]], [[1ht3]] – EaPRO + Ca + Hg <br />
[[2pkc]] – EaPRO + Na  <br />
[[4dj5]] – EaPRO  <br />
 
''PRO K complex with peptide''
 
[[3prk]], [[1p7v]], [[1p7w]] – EaPRO + Ca + peptide inhibitor  <br />
[[1bjr]], [[2dqk]], [[2duj]] – EaPRO + Ca + lactoferrin peptide  <br />
[[2hd4]] – EaPRO + Ca + lactoferrin peptide inhibitor<br />
[[2dp4]], [[3ptl]] – EaPRO + lactoferrin peptide  <br />
[[1pek]], [[1pfg]] – EaPRO + peptide inhibitor  <br />
[[1pj8]] – EaPRO + Hg + substrate analog peptide  <br />
[[2hpz]], [[2pq2]] – EaPRO + Ca + peptide  <br />
[[3osz]] – EaPRO + Ca + antimicrobial peptide  <br />
[[2b6n]] – PRO + tripeptide - ''Serratia''<br />


''PRO K complex with small molecule''
[[2pwb]] – EaPRO + Ca + coumarin  <br />
[[2pyz]] – EaPRO + Ca + auramine  <br />
[[2pwa]] – EaPRO + Ca + alanine boronic acid  <br />
[[1oyo]] – EaPRO + Ca + melanin monomer  <br />
[[3dyb]] – EaPRO + Ca + digalacturonic acid  <br />
===PRO 3C===
[[1qa7]] – PRO – Hepatitis virus<br />
[[2vb0]] - PRO – Coxsakievirus
===H2-PRO===
[[1wni]] – PRO – ''Trimeresurus flavoviridis''
===Aspartic PRO===
[[2asi]] – PRO – ''Rhizomucor miehei''<br />
[[1zap]] – CaPRO – ''Candida albicans''<br />
[[1izd]] - AoPRO – ''Aspergillus oryzae''<br />
[[1eag]] – CaPRO + inhibitor <br />
[[1fq4]] - yPRO + inhibitor<br />
[[1j71]] - PRO + polypeptide inhibitor – ''Candida tropicalis''<br />
[[1ize]] - AoPRO + polypeptide-statin inhibitor<br />
[[1wkr]] - PRO + polypeptide-statin inhibitor – ''Irpex lacteus''
===Cysteine PRO===
[[2hrv]] – PRO 2A – human rhinovirus
===Serine PRO===
[[1s2n]], [[1sh7]] – PRO – ''Vibrio''<br />
[[3s9a]], [[3s9b]] – RvPRO – Siamese Russell’s viper<br />
[[3s9c]], [[3sbk]] – RvPRO + human factor V polypeptide<br />
[[1ga1]], [[1ga4]], [[1ga6]], [[1nlu]] – PsPRO + iodotyrostatin fragment – ''Pseudomonas''<br />
[[1kdv]], [[1kdy]], [[1kdz]], [[1ke1]], [[1ke2]] - PsPRO + polypeptide inhibitor
</StructureSection>
== References ==
== References ==
<references/>
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Latest revision as of 22:45, 26 January 2025

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