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| | <StructureSection load='' size='350' side='right' scene='Journal:JBSD:39/Cv/11' caption=''> |
| | __TOC__ |
| | ==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=''>
| | '''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. 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). | | * '''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]]. |
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| ==3D structures of proteinase== | | ==3D structures of proteinase== |
| | [[Proteinase 3D structures]] |
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| Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
| | </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>
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| == References == | | == References == |
| <references/> | | <references/> |
| [[Category: Topic Page]] | | [[Category: Topic Page]] |