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
- ↑ 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
- ↑ Mechler B, Wolf DH. Analysis of proteinase A function in yeast. Eur J Biochem. 1981 Dec;121(1):47-52. PMID:6799292
- ↑ 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:https://dx.doi.org/10.1006/abio.1998.2655
- ↑ 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
- ↑ 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:https://dx.doi.org/10.1002/yea.1485
- ↑ 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:https://dx.doi.org/10.1007/978-1-4419-8414-2_3
