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 on PRO B 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 01:45, 27 January 2025

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.

  • PRO B is a serine protease[1]. For more details see Streptomyces griseus proteinase B.
  • PRO A is a carboxylproteinase[2].
  • PRO K is a serine protease which cleaves proteins preferentially after hydrophobic residues[3]. 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).
  • Endothiapepsin is an aspartic PRO from Cryphonectria parasitica[4].
  • Saccharopepsin is an aspartic PRO from yeast[5].
  • Falcipain is an cystein PRO from Plasmodium falciparum[6].

For cysteine PRO from Trypanosoma cruzi see Cruzain.

3D structures of proteinase

Proteinase 3D structures


Drag the structure with the mouse to rotate

ReferencesReferences

  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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