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=''>
+<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.  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).
+__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 />
+*  '''PRO B''' is a serine protease<ref>PMID:3325823</ref>.  For more details see [[Streptomyces griseus proteinase B]].<br />
+*  '''PRO A''' is a carboxylproteinase<ref>PMID:6799292</ref>.<br />
+*  '''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==
+[[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/>
 [[Category: Topic Page]]