Proteinase

From Proteopedia

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 3D structures of proteinase 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

References

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