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='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=''> | ||
'''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. 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). | '''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 A''' is a carboxylproteinase.<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). | |||
==3D structures of proteinase== | ==3D structures of proteinase== |
Revision as of 10:43, 20 August 2014
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.
3D structures of proteinaseUpdated on 01-June-2025 PRO A2sga – SgPRO – Streptomyces griseus 2jxr, 1fmu, 1fmx – yPRO - yeast PRO B3sgb – SgPRO + turkey ovomucoid inhibitor 1sgp, 1sgq, 1sgr, 1cso, 1ct0, 1ct2, 1ct4, 1ds2, 2sgp, 2nu3, 2nu4 – SgPRO + turkey ovomucoid inhibitor (mutant) PRO K2prk, 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 1ic6 – EaPRO (mutant) + Ca PRO K complex with peptide 3prk, 1p7v, 1p7w – EaPRO + Ca + peptide inhibitor 1bjr, 2dqk, 2duj – EaPRO + Ca + lactoferrin peptide PRO K complex with small molecule 2pwb – EaPRO + Ca + coumarin 2pyz – EaPRO + Ca + auramine PRO 3C1qa7 – PRO – Hepatitis virus 2vb0 - PRO – Coxsakievirus H2-PRO1wni – PRO – Trimeresurus flavoviridis Aspartic PRO2asi – PRO – Rhizomucor miehei 1zap – CaPRO – Candida albicans Cysteine PRO2hrv – PRO 2A – human rhinovirus Serine PRO3s9a, 3s9b – RvPRO – Siamese Russell’s viper
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