Proteinase

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(New page: <StructureSection load='2duj' size='340' side='right' caption='E. coli proteinase K complex with lactoferrin peptide and Ca+2 (PDB code 2duj)' scene=''> '''Proteinase''' (PRO) are enz...)
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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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<StructureSection load='2duj' size='340' side='right' caption='E. coli proteinase K complex with lactoferrin peptide and Ca+2 (PDB code [[2duj]])' scene=''>
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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 />
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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. PRO B is a serine protease. For more details on PRO B see [[Streptomyces griseus proteinase B]]. PRO A is a carboxylproteinase. Proteinase K (PRO) is a serine protease which cleaves proteins preferentially after hydrophobic residues. Calcium ions contribute to the stability of the enzyme. PRO is active over a wide pH range and is used in molecular biology to inactivate nucleases from preparations of DNA or RNA. PRO 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 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<ref>PMID:6799292</ref>.<br />
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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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*'''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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'''PRO A'''
 
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2sga – SgPRO – ''Streptomyces griseus''
 
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2jxr, 1fmu, 1fmx – yPRO - yeast
 
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1sgc - SgPRO + chymostatin A
 
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3sga, 4sga, 5sga - SgPRO + polypeptide inhibitor
 
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1dp5, 1dpj, 1g0v - yPRO + polypeptide inhibitor IA3
 
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1fq5 - yPRO + inhibitor
 
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'''PRO B'''
 
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3sgb – SgPRO + turkey ovomucoid inhibitor
 
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1sgp, 1sgq, 1sgr, 1cso, 1ct0, 1ct2, 1ct4, 1ds2, 2sgp, 2nu3, 2nu4 – SgPRO + turkey ovomucoid inhibitor (mutant)
 
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4sgb - SgPRO + potato inhibitor
 
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'''PRO 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]] – EaPRO <br />
 
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''PRO 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]] – 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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''PRO 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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'''PRO 3C'''
 
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1qa7 – PRO – Hepatitis virus
 
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2vb0 - PRO – Coxsakievirus
 
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'''H2-PRO'''
 
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1wni – PRO – ''Trimeresurus flavoviridis''
 
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'''Aspartic PRO'''
 
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2asi – PRO – ''Rhizomucor miehei''
 
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1zap – CaPRO – ''Candida albicans''
 
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1izd - AoPRO – ''Aspergillus oryzae''
 
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1eag – CaPRO + inhibitor
 
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1fq4 - yPRO + inhibitor
 
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1j71 - PRO + polypeptide inhibitor – ''Candida tropicalis''
 
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1ize - AoPRO + polypeptide-statine inhibitor
 
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1wkr - PRO + polypeptide-statine inhibitor – ''Irpex lacteus''
 
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'''Cysteine PRO'''
 
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2hrv – PRO 2A – human rhinovirus
 
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'''Serine PRO'''
 
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1s2n, 1sh7 – PRO – Vibrio
 
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3s9a, 3s9b – RvPRO – Siamese Russell’s viper
 
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3s9c, 3sbk – RvPRO + human factor V polypeptide
 
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1ga1, 1ga4, 1ga6, 1nlu – PsPRO + iodotyrostatin fragment – ''Pseudomonas''
 
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1kdv, 1kdy, 1kdz, 1ke1, 1ke2 - PsPRO + polypeptide inhibitor
 
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</StructureSection>
 
== 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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