Proteinase: Difference between revisions
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* '''PRO A''' is a carboxylproteinase<ref>PMID:6799292</ref>.<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). | * '''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). | ||
For cysteine PRO from ''Trypanosoma cruzi'' see [[Cruzain]]. | |||
=== The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen-bond density in the reactive loop <ref>doi 10.1080/07391102.2012.745378</ref> === | === The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen-bond density in the reactive loop <ref>doi 10.1080/07391102.2012.745378</ref> === | ||
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**[[1wkr]] - PRO + polypeptide-statin inhibitor – ''Irpex lacteus'' | **[[1wkr]] - PRO + polypeptide-statin inhibitor – ''Irpex lacteus'' | ||
*'''Cysteine Proteinase''' | *'''Cysteine Proteinase''' or '''gingipain''' | ||
**[[2hrv]] – PRO 2A – human rhinovirus | **[[2hrv]] – PRO 2A – human rhinovirus<br /> | ||
**[[3m1h]], [[4itc]] – PgPRO adhesion domain residues 982-1154 – ''Porphyromonas gingivalis'' <br /> | |||
**[[4rbm]], [[4tkx]] – PgPRO catalytic domain residues 229-683<br /> | |||
**[[5mun]] – PgPRO residues 20-228 <br /> | |||
**[[2fo5]] – PRO residues 133-356 + leupeptin – ''Hordenum vulgare'' <br /> | |||
**[[2e03]], [[2e02]], [[2e01]], [[2e00]], [[2dzz]], [[2dzy]] – yPRO 1 (mutant) <br /> | |||
**[[1x9y]] – SaPRO – ''Staphylococcus aureus'' <br /> | |||
**[[1y4h]], [[1pxv]] – SaPRO + PRO inhibitor <br /> | |||
*'''Serine Proteinase''' | *'''Serine Proteinase''' | ||
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**[[1s2n]], [[1sh7]] – PRO – ''Vibrio''<br /> | **[[1s2n]], [[1sh7]] – PRO – ''Vibrio''<br /> | ||
**[[3s9a]], [[3s9b]] – RvPRO – Siamese Russell’s viper<br /> | **[[3s9a]], [[3s9b]] – RvPRO – Siamese Russell’s viper<br /> | ||
**[[1po0]], [[1op2]] – PRO – Chinese moccasin <br /> | |||
**[[1qy8]] – SaPRO <br /> | |||
**[[1mbm]] – PRO – equine arteritis virus <br /> | |||
**[[1dbi]] – PRO – ''Bacillus'' <br /> | |||
**[[3s9c]], [[3sbk]] – RvPRO + human factor V polypeptide<br /> | **[[3s9c]], [[3sbk]] – RvPRO + human factor V polypeptide<br /> | ||
**[[1ga1]], [[1ga4]], [[1ga6]], [[1nlu]] – PsPRO + iodotyrostatin fragment – ''Pseudomonas''<br /> | **[[1ga1]], [[1ga4]], [[1ga6]], [[1nlu]] – PsPRO + iodotyrostatin fragment – ''Pseudomonas''<br /> | ||
**[[1kdv]], [[1kdy]], [[1kdz]], [[1ke1]], [[1ke2]] - PsPRO + polypeptide inhibitor | **[[1kdv]], [[1kdy]], [[1kdz]], [[1ke1]], [[1ke2]] - PsPRO + polypeptide inhibitor<br /> | ||
**[[5m3n]], [[1lcy]] – hPRO HTRA2 – human <br /> | |||
**[[5fht]], [[5m3o]], [[5tny]], [[5tnz]], [[5to0]], [[5to1]], [[5wyn]] – hPRO HTRA2 (mutant) <br /> | |||
}} | }} | ||