Proteinase

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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=''>
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<StructureSection load='' size='350' side='right' scene='Journal:JBSD:39/Cv/11' caption=''>
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__TOC__
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==Function==
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'''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 />
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* '''PRO B''' is a serine protease. For more details see [[Streptomyces griseus proteinase B]].<br />
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* '''PRO B''' is a serine protease<ref>PMID:3325823</ref>. For more details see [[Streptomyces griseus proteinase B]].<br />
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* '''PRO A''' is a carboxylproteinase.<br />
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* '''PRO A''' is a carboxylproteinase<ref>PMID:6799292</ref>.<br />
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* '''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).
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* '''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 />
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</StructureSection>
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*'''Endothiapepsin''' is an '''aspartic PRO''' from ''Cryphonectria parasitica''<ref>PMID:1525155</ref>.<br />
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*'''Saccharopepsin''' is an '''aspartic PRO''' from yeast<ref>PMID:17447722</ref>.<br />
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*'''Falcipain''' is an '''cystein PRO''' from ''Plasmodium falciparum''<ref>PMID:21660657</ref>.<br />
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For '''cysteine PRO''' from ''Trypanosoma cruzi'' see [[Cruzain]].
==3D structures of proteinase==
==3D structures of proteinase==
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[[Proteinase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*'''Proteinase A'''
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**[[2sga]] – SgPRO – ''Streptomyces griseus''<br />
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**[[2jxr]], [[1fmu]], [[1fmx]] – yPRO - yeast<br />
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**[[1sgc]] - SgPRO + chymostatin A<br />
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**[[3sga]], [[4sga]], [[5sga]] - SgPRO + polypeptide inhibitor<br />
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**[[1dp5]], [[1dpj]], [[1g0v]] - yPRO + polypeptide inhibitor IA3<br />
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**[[1fq5]] - yPRO + inhibitor<br />
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**[[4fvd]] – hevPRO 2A + peptide – human enterovirus <br />
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**[[4fvb]] – hevPRO 2A (mutant) <br />
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*'''Proteinase B'''
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**[[3sgb]] – SgPRO + turkey ovomucoid inhibitor<br />
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**[[1sgp]], [[1sgq]], [[1sgr]], [[1cso]], [[1ct0]], [[1ct2]], [[1ct4]], [[1ds2]], [[2sgp]], [[2nu3]], [[2nu4]] – SgPRO + turkey ovomucoid inhibitor (mutant)<br />
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**[[4sgb]] - SgPRO + potato inhibitor
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*'''Proteinase K'''
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**[[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 />
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**[[1ic6]] – EaPRO (mutant) + Ca <br />
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**[[1ptk]], [[1ht3]] – EaPRO + Ca + Hg <br />
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**[[2pkc]] – EaPRO + Na <br />
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**[[4dj5]], [[4woc]], [[4wob]] – EaPRO <br />
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*Proteinase K complex with peptide
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**[[3prk]], [[1p7v]], [[1p7w]] – EaPRO + Ca + peptide inhibitor <br />
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**[[1bjr]], [[2dqk]], [[2duj]] – EaPRO + Ca + lactoferrin peptide <br />
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**[[2hd4]] – EaPRO + Ca + lactoferrin peptide inhibitor<br />
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**[[2dp4]], [[3ptl]] – EaPRO + lactoferrin peptide <br />
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**[[1pek]], [[1pfg]], [[4zar]] – EaPRO + peptide inhibitor <br />
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**[[1pj8]] – EaPRO + Hg + substrate analog peptide <br />
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**[[2hpz]], [[2pq2]] – EaPRO + Ca + peptide <br />
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**[[3osz]] – EaPRO + Ca + antimicrobial peptide <br />
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**[[2b6n]] – PRO + tripeptide - ''Serratia''<br />
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*Proteinase K complex with small molecule
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**[[2pwb]] – EaPRO + Ca + coumarin <br />
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**[[2pyz]] – EaPRO + Ca + auramine <br />
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**[[2pwa]] – EaPRO + Ca + alanine boronic acid <br />
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**[[1oyo]] – EaPRO + Ca + melanin monomer <br />
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**[[3dyb]] – EaPRO + Ca + digalacturonic acid <br />
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*'''Proteinase 3C'''
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**[[1qa7]] – PRO – Hepatitis virus<br />
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**[[2vb0]], [[3zyd]] - PRO – Coxsakievirus<br />
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**[[3zye]] – csvPRO (mutant) <br />
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**[[3zzd]], [[3zzc]], [[3zza]], [[3zzb]], [[3zz8]], [[3zz9]], [[3zz7]], [[3zz5]], [[3zz3]], [[3zz4]] – csvPRO (mutant) + inhibitor <br />
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**[[4ghq]] – hevPRO <br />
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**[[4ght]] – hevPRO + common cold drug <br />
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*'''H2-Proteinase'''
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**[[1wni]] – PRO – ''Trimeresurus flavoviridis''
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*'''Aspartic Proteinase'''
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**[[2asi]] – PRO – ''Rhizomucor miehei''<br />
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**[[1zap]] – CaPRO – ''Candida albicans''<br />
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**[[1izd]] - AoPRO – ''Aspergillus oryzae''<br />
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**[[1eag]] – CaPRO + inhibitor <br />
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**[[1fq4]] - yPRO + inhibitor<br />
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**[[1j71]] - PRO + polypeptide inhibitor – ''Candida tropicalis''<br />
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**[[1ize]] - AoPRO + polypeptide-statin inhibitor<br />
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**[[1wkr]] - PRO + polypeptide-statin inhibitor – ''Irpex lacteus''
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*'''Cysteine Proteinase'''
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**[[2hrv]] – PRO 2A – human rhinovirus
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*'''Serine Proteinase'''
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**[[1s2n]], [[1sh7]] – PRO – ''Vibrio''<br />
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**[[3s9a]], [[3s9b]] – RvPRO – Siamese Russell’s viper<br />
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**[[3s9c]], [[3sbk]] – RvPRO + human factor V polypeptide<br />
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**[[1ga1]], [[1ga4]], [[1ga6]], [[1nlu]] – PsPRO + iodotyrostatin fragment – ''Pseudomonas''<br />
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**[[1kdv]], [[1kdy]], [[1kdz]], [[1ke1]], [[1ke2]] - PsPRO + polypeptide inhibitor
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}}
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== References ==
== References ==
<references/>
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

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References

  1. ↑ Moehle CM, Tizard R, Lemmon SK, Smart J, Jones EW. Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases. Mol Cell Biol. 1987 Dec;7(12):4390-9. PMID:3325823
  2. ↑ Mechler B, Wolf DH. Analysis of proteinase A function in yeast. Eur J Biochem. 1981 Dec;121(1):47-52. PMID:6799292
  3. ↑ Petsch D, Deckwer WD, Anspach FB. Proteinase K digestion of proteins improves detection of bacterial endotoxins by the Limulus amebocyte lysate assay: application for endotoxin removal from cationic proteins. Anal Biochem. 1998 May 15;259(1):42-7. doi: 10.1006/abio.1998.2655. PMID:9606141 doi:http://dx.doi.org/10.1006/abio.1998.2655
  4. ↑ Cooper J, Quail W, Frazao C, Foundling SI, Blundell TL, Humblet C, Lunney EA, Lowther WT, Dunn BM. X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors. Biochemistry. 1992 Sep 8;31(35):8142-50. PMID:1525155
  5. ↑ Parr CL, Keates RA, Bryksa BC, Ogawa M, Yada RY. The structure and function of Saccharomyces cerevisiae proteinase A. Yeast. 2007 Jun;24(6):467-80. doi: 10.1002/yea.1485. PMID:17447722 doi:http://dx.doi.org/10.1002/yea.1485
  6. ↑ Rosenthal PJ. Falcipains and other cysteine proteases of malaria parasites. Adv Exp Med Biol. 2011;712:30-48. doi: 10.1007/978-1-4419-8414-2_3. PMID:21660657 doi:http://dx.doi.org/10.1007/978-1-4419-8414-2_3

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