Proteinase

spinqualitylabelsall models E. coli proteinase K complex with lactoferrin peptide and Ca+2 (PDB code 2duj) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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). 3D structures of proteinase Updated on 16-April-2014 PRO A 2sga – SgPRO – Streptomyces griseus 2jxr, 1fmu, 1fmx – yPRO - yeast 1sgc - SgPRO + chymostatin A 3sga, 4sga, 5sga - SgPRO + polypeptide inhibitor 1dp5, 1dpj, 1g0v - yPRO + polypeptide inhibitor IA3 1fq5 - yPRO + inhibitor PRO B 3sgb – SgPRO + turkey ovomucoid inhibitor 1sgp, 1sgq, 1sgr, 1cso, 1ct0, 1ct2, 1ct4, 1ds2, 2sgp, 2nu3, 2nu4 – SgPRO + turkey ovomucoid inhibitor (mutant) 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 1ic6 – EaPRO (mutant) + Ca 1ptk, 1ht3 – EaPRO + Ca + Hg 2pkc – EaPRO + Na 4dj5 – EaPRO PRO K complex with peptide 3prk, 1p7v, 1p7w – EaPRO + Ca + peptide inhibitor 1bjr, 2dqk, 2duj – EaPRO + Ca + lactoferrin peptide 2hd4 – EaPRO + Ca + lactoferrin peptide inhibitor 2dp4, 3ptl – EaPRO + lactoferrin peptide 1pek, 1pfg – EaPRO + peptide inhibitor 1pj8 – EaPRO + Hg + substrate analog peptide 2hpz, 2pq2 – EaPRO + Ca + peptide 3osz – EaPRO + Ca + antimicrobial peptide 2b6n – PRO + tripeptide - Serratia PRO K complex with small molecule 2pwb – EaPRO + Ca + coumarin 2pyz – EaPRO + Ca + auramine 2pwa – EaPRO + Ca + alanine boronic acid 1oyo – EaPRO + Ca + melanin monomer 3dyb – EaPRO + Ca + digalacturonic acid PRO 3C 1qa7 – PRO – Hepatitis virus 2vb0 - PRO – Coxsakievirus H2-PRO 1wni – PRO – Trimeresurus flavoviridis Aspartic PRO 2asi – PRO – Rhizomucor miehei 1zap – CaPRO – Candida albicans 1izd - AoPRO – Aspergillus oryzae 1eag – CaPRO + inhibitor 1fq4 - yPRO + inhibitor 1j71 - PRO + polypeptide inhibitor – Candida tropicalis 1ize - AoPRO + polypeptide-statine inhibitor 1wkr - PRO + polypeptide-statine inhibitor – Irpex lacteus Cysteine PRO 2hrv – PRO 2A – human rhinovirus Serine PRO 1s2n, 1sh7 – PRO – Vibrio 3s9a, 3s9b – RvPRO – Siamese Russell’s viper 3s9c, 3sbk – RvPRO + human factor V polypeptide 1ga1, 1ga4, 1ga6, 1nlu – PsPRO + iodotyrostatin fragment – Pseudomonas 1kdv, 1kdy, 1kdz, 1ke1, 1ke2 - PsPRO + polypeptide inhibitor

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Alexander Berchansky, Michal Harel, Joel L. Sussman, Karsten Theis